RL4_ECOLI
ID RL4_ECOLI Reviewed; 201 AA.
AC P60723; P02388; Q2M6Y4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=50S ribosomal protein L4;
DE AltName: Full=Large ribosomal subunit protein uL4 {ECO:0000303|PubMed:24524803};
GN Name=rplD; Synonyms=eryA; OrderedLocusNames=b3319, JW3281;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE, AND SUBUNIT.
RA Kimura M., Wittmann-Liebold B.;
RT "The primary structure of protein L4 from the large subunit of the
RT Escherichia coli ribosome.";
RL FEBS Lett. 121:317-322(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3892488; DOI=10.1093/nar/13.12.4521;
RA Zurawski G., Zurawski S.M.;
RT "Structure of the Escherichia coli S10 ribosomal protein operon.";
RL Nucleic Acids Res. 13:4521-4526(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 26-50, SUBUNIT, AND CROSS-LINKING TO RRNA.
RC STRAIN=MRE-600;
RX PubMed=7556101; DOI=10.1002/j.1460-2075.1995.tb00137.x;
RA Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.;
RT "Protein-rRNA binding features and their structural and functional
RT implications in ribosomes as determined by cross-linking studies.";
RL EMBO J. 14:4578-4588(1995).
RN [7]
RP CROSS-LINKING TO 23S RRNA.
RC STRAIN=MRE-600;
RX PubMed=6170935; DOI=10.1093/nar/9.17.4285;
RA Wower I., Wower J., Meinke M., Brimacombe R.;
RT "The use of 2-iminothiolane as an RNA-protein cross-linking agent in
RT Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-
RT linked to proteins L4, L6, L21, L23, L27 and L29.";
RL Nucleic Acids Res. 9:4285-4302(1981).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [10]
RP CHARACTERIZATION OF AN ERYTHROMYCIN-RESISTANT VARIANT.
RC STRAIN=N282;
RX PubMed=4589347; DOI=10.1007/bf00333665;
RA Wittmann H.G., Stoffler G., Apirion D., Rosen L., Tanaka K., Tamaki M.,
RA Takata R., Dekio S., Otaka E.;
RT "Biochemical and genetic studies on two different types of erythromycin
RT resistant mutants of Escherichia coli with altered ribosomal proteins.";
RL Mol. Gen. Genet. 127:175-189(1973).
RN [11]
RP ASSEMBLY MAP OF THE 50S SUBUNIT, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=3298242; DOI=10.1016/s0021-9258(18)47489-3;
RA Herold M., Nierhaus K.H.;
RT "Incorporation of six additional proteins to complete the assembly map of
RT the 50 S subunit from Escherichia coli ribosomes.";
RL J. Biol. Chem. 262:8826-8833(1987).
RN [12]
RP FUNCTION IN TRANSCRIPTION/TRANSLATION REGULATION.
RC STRAIN=K12 / LL308;
RX PubMed=2442760; DOI=10.1073/pnas.84.18.6516;
RA Freedman L.P., Zengel J.M., Archer R.H., Lindahl L.;
RT "Autogenous control of the S10 ribosomal protein operon of Escherichia
RT coli: genetic dissection of transcriptional and posttranscriptional
RT regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6516-6520(1987).
RN [13]
RP MECHANISM OF TRANSCRIPTIONAL REGULATION.
RC STRAIN=K12 / LL308;
RX PubMed=1692593; DOI=10.1016/s0022-2836(05)80122-6;
RA Zengel J.M., Lindahl L.;
RT "Escherichia coli ribosomal protein L4 stimulates transcription termination
RT at a specific site in the leader of the S10 operon independent of L4-
RT mediated inhibition of translation.";
RL J. Mol. Biol. 213:67-78(1990).
RN [14]
RP REQUIREMENT FOR NUSA IN TRANSCRIPTION TERMINATION CONTROL.
RX PubMed=2157208; DOI=10.1073/pnas.87.7.2675;
RA Zengel J.M., Lindahl L.;
RT "Ribosomal protein L4 stimulates in vitro termination of transcription at a
RT NusA-dependent terminator in the S10 operon leader.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2675-2679(1990).
RN [15]
RP IDENTIFICATION OF CHANGES IN AN ERYTHROMYCIN-RESISTANT VARIANT.
RC STRAIN=N282;
RX PubMed=7928988; DOI=10.1128/jb.176.20.6192-6198.1994;
RA Chittum H.S., Champney W.S.;
RT "Ribosomal protein gene sequence changes in erythromycin-resistant mutants
RT of Escherichia coli.";
RL J. Bacteriol. 176:6192-6198(1994).
RN [16]
RP ERYTHROMYCIN AND RIBOSOME ASSEMBLY.
RC STRAIN=N282, and SK901;
RX PubMed=7766155; DOI=10.1007/bf00295501;
RA Chittum H.S., Champney W.S.;
RT "Erythromycin inhibits the assembly of the large ribosomal subunit in
RT growing Escherichia coli cells.";
RL Curr. Microbiol. 30:273-279(1995).
RN [17]
RP REQUIREMENT FOR RNA-BINDING, MUTAGENESIS, AND REGULATION-DEFECTIVE MUTANTS.
RC STRAIN=K12 / LL308;
RX PubMed=8846294;
RA Li X., Lindahl L., Zengel J.M.;
RT "Ribosomal protein L4 from Escherichia coli utilizes nonidentical
RT determinants for its structural and regulatory functions.";
RL RNA 2:24-37(1996).
RN [18]
RP ABILITY TO REGULATE S10 OPERON EXPRESSION IN OTHER BACTERIA.
RC STRAIN=K12 / LL308;
RX PubMed=10498727; DOI=10.1128/jb.181.19.6124-6132.1999;
RA Allen T., Shen P., Samsel L., Liu R., Lindahl L., Zengel J.M.;
RT "Phylogenetic analysis of L4-mediated autogenous control of the S10
RT ribosomal protein operon.";
RL J. Bacteriol. 181:6124-6132(1999).
RN [19]
RP REQUIREMENT FOR RIBOSOME ASSEMBLY, AND S10 OPERON REGULATION.
RC STRAIN=K12 / LL308;
RX PubMed=13130133; DOI=10.1261/rna.5400703;
RA Zengel J.M., Jerauld A., Walker A., Wahl M.C., Lindahl L.;
RT "The extended loops of ribosomal proteins L4 and L22 are not required for
RT ribosome assembly or L4-mediated autogenous control.";
RL RNA 9:1188-1197(2003).
RN [20]
RP MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX PubMed=10094780; DOI=10.1006/abio.1998.3077;
RA Arnold R.J., Reilly J.P.;
RT "Observation of Escherichia coli ribosomal proteins and their
RT posttranslational modifications by mass spectrometry.";
RL Anal. Biochem. 269:105-112(1999).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=12809609; DOI=10.1016/s0092-8674(03)00427-6;
RA Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
RA Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.;
RT "Study of the structural dynamics of the E. coli 70S ribosome using real-
RT space refinement.";
RL Cell 113:789-801(2003).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (17.8 ANGSTROMS), SUBUNIT, AND EFFECT OF
RP THE ERYTHROMYCIN-RESISTANT VARIANT ON THE POLYPEPTIDE EXIT TUNNEL.
RC STRAIN=N282;
RX PubMed=11511371; DOI=10.1016/s1097-2765(01)00293-3;
RA Gabashvili I.S., Gregory S.T., Valle M., Grassucci R., Worbs M., Wahl M.C.,
RA Dahlberg A.E., Frank J.;
RT "The polypeptide tunnel system in the ribosome and its gating in
RT erythromycin resistance mutants of L4 and L22.";
RL Mol. Cell 8:181-188(2001).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES,
RP AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=16272117; DOI=10.1126/science.1117230;
RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A.,
RA Holton J.M., Cate J.H.D.;
RT "Structures of the bacterial ribosome at 3.5 A resolution.";
RL Science 310:827-834(2005).
RN [24]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF TNAC-STALLED 50S
RP RIBOSOMAL SUBUNIT, AND SUBUNIT.
RC STRAIN=K12 / A19 / KC6;
RX PubMed=25310980; DOI=10.1016/j.celrep.2014.09.011;
RA Bischoff L., Berninghausen O., Beckmann R.;
RT "Molecular basis for the ribosome functioning as an L-tryptophan sensor.";
RL Cell Rep. 9:469-475(2014).
RN [25]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.5 ANGSTROMS) OF 50S RIBOSOMAL SUBUNIT
RP IN COMPLEX WITH OBGE AND GMP-PNP, AND SUBUNIT.
RX PubMed=24844575; DOI=10.1371/journal.pbio.1001866;
RA Feng B., Mandava C.S., Guo Q., Wang J., Cao W., Li N., Zhang Y., Zhang Y.,
RA Wang Z., Wu J., Sanyal S., Lei J., Gao N.;
RT "Structural and functional insights into the mode of action of a
RT universally conserved Obg GTPase.";
RL PLoS Biol. 12:E1001866-E1001866(2014).
RN [26]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906160; DOI=10.1038/nature20822;
RA Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT "Mechanistic insights into the alternative translation termination by ArfA
RT and RF2.";
RL Nature 541:550-553(2017).
RN [27]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906161; DOI=10.1038/nature20821;
RA Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R.,
RA Wilson D.N.;
RT "Structural basis for ArfA-RF2-mediated translation termination on mRNAs
RT lacking stop codons.";
RL Nature 541:546-549(2017).
RN [28]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27934701; DOI=10.1126/science.aai9127;
RA James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
RT "Translational termination without a stop codon.";
RL Science 354:1437-1440(2016).
RN [29]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=28077875; DOI=10.1038/nature21053;
RA Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA Jin H.;
RT "Structural basis of co-translational quality control by ArfA and RF2 bound
RT to ribosome.";
RL Nature 541:554-557(2017).
CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein
CC initially binds near the 5'-end of the 23S rRNA (PubMed:3298242). It is
CC important during the early stages of 50S assembly (PubMed:3298242). It
CC makes multiple contacts with different domains of the 23S rRNA in the
CC assembled 50S subunit and ribosome (PubMed:7556101, PubMed:6170935).
CC {ECO:0000269|PubMed:13130133, ECO:0000269|PubMed:2442760,
CC ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:6170935,
CC ECO:0000269|PubMed:7556101}.
CC -!- FUNCTION: Protein L4 is a both a transcriptional repressor and a
CC translational repressor protein; these two functions are independent of
CC each other. It regulates transcription of the S10 operon (to which L4
CC belongs) by causing premature termination of transcription within the
CC S10 leader; termination absolutely requires the NusA protein. L4
CC controls the translation of the S10 operon by binding to its mRNA. The
CC regions of L4 that control regulation (residues 131-210) are different
CC from those required for ribosome assembly (residues 89-103).
CC {ECO:0000269|PubMed:13130133, ECO:0000269|PubMed:1692593,
CC ECO:0000269|PubMed:2157208, ECO:0000269|PubMed:2442760}.
CC -!- FUNCTION: Forms part of the polypeptide exit tunnel.
CC {ECO:0000269|PubMed:11511371, ECO:0000269|PubMed:2442760}.
CC -!- FUNCTION: Can regulate expression from Citrobacter freundii,
CC Haemophilus influenzae, Morganella morganii, Salmonella typhimurium,
CC Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but
CC not Pseudomonas aeruginosa) S10 leaders in vitro.
CC {ECO:0000269|PubMed:10498727}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (Ref.1, PubMed:7556101,
CC PubMed:3298242, PubMed:10094780, PubMed:12809609, PubMed:11511371,
CC PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701,
CC PubMed:27906160, PubMed:27906161). {ECO:0000269|PubMed:10094780,
CC ECO:0000269|PubMed:11511371, ECO:0000269|PubMed:12809609,
CC ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:24844575,
CC ECO:0000269|PubMed:25310980, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:7556101,
CC ECO:0000269|Ref.1}.
CC -!- INTERACTION:
CC P60723; P0A6I6: coaD; NbExp=2; IntAct=EBI-545597, EBI-553173;
CC P60723; P0A6K3: def; NbExp=4; IntAct=EBI-545597, EBI-548913;
CC -!- MASS SPECTROMETRY: Mass=22086.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- MISCELLANEOUS: The erythromycin sensitive allele is dominant over the
CC resistant allele.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000305}.
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DR EMBL; X02613; CAA26461.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58116.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76344.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77972.1; -; Genomic_DNA.
DR PIR; C23129; R5EC4.
DR RefSeq; NP_417778.1; NC_000913.3.
DR RefSeq; WP_000424395.1; NZ_STEB01000038.1.
DR PDB; 2J28; EM; 8.00 A; E=1-201.
DR PDB; 2RDO; EM; 9.10 A; E=1-201.
DR PDB; 3BBX; EM; 10.00 A; E=1-201.
DR PDB; 3J5L; EM; 6.60 A; E=1-201.
DR PDB; 3J7Z; EM; 3.90 A; E=1-201.
DR PDB; 3J8G; EM; 5.00 A; E=1-201.
DR PDB; 3J9Y; EM; 3.90 A; E=1-201.
DR PDB; 3J9Z; EM; 3.60 A; L6=1-201.
DR PDB; 3JA1; EM; 3.60 A; LF=1-201.
DR PDB; 3JBU; EM; 3.64 A; e=1-201.
DR PDB; 3JBV; EM; 3.32 A; e=1-201.
DR PDB; 3JCD; EM; 3.70 A; E=1-201.
DR PDB; 3JCE; EM; 3.20 A; E=1-201.
DR PDB; 3JCJ; EM; 3.70 A; D=1-201.
DR PDB; 3JCN; EM; 4.60 A; E=1-201.
DR PDB; 4CSU; EM; 5.50 A; E=1-201.
DR PDB; 4U1U; X-ray; 2.95 A; BE/DE=1-201.
DR PDB; 4U1V; X-ray; 3.00 A; BE/DE=1-201.
DR PDB; 4U20; X-ray; 2.90 A; BE/DE=1-201.
DR PDB; 4U24; X-ray; 2.90 A; BE/DE=1-201.
DR PDB; 4U25; X-ray; 2.90 A; BE/DE=1-201.
DR PDB; 4U26; X-ray; 2.80 A; BE/DE=1-201.
DR PDB; 4U27; X-ray; 2.80 A; BE/DE=1-201.
DR PDB; 4UY8; EM; 3.80 A; E=1-201.
DR PDB; 4V47; EM; 12.30 A; AC=1-201.
DR PDB; 4V48; EM; 11.50 A; AC=1-201.
DR PDB; 4V4H; X-ray; 3.46 A; BE/DE=1-201.
DR PDB; 4V4Q; X-ray; 3.46 A; BE/DE=1-201.
DR PDB; 4V4V; EM; 15.00 A; BC=1-198.
DR PDB; 4V4W; EM; 15.00 A; BC=1-198.
DR PDB; 4V50; X-ray; 3.22 A; BE/DE=1-201.
DR PDB; 4V52; X-ray; 3.21 A; BE/DE=1-201.
DR PDB; 4V53; X-ray; 3.54 A; BE/DE=1-201.
DR PDB; 4V54; X-ray; 3.30 A; BE/DE=1-201.
DR PDB; 4V55; X-ray; 4.00 A; BE/DE=1-201.
DR PDB; 4V56; X-ray; 3.93 A; BE/DE=1-201.
DR PDB; 4V57; X-ray; 3.50 A; BE/DE=1-201.
DR PDB; 4V5B; X-ray; 3.74 A; AE/CE=1-201.
DR PDB; 4V5H; EM; 5.80 A; BE=1-201.
DR PDB; 4V5Y; X-ray; 4.45 A; BE/DE=1-201.
DR PDB; 4V64; X-ray; 3.50 A; BE/DE=1-201.
DR PDB; 4V65; EM; 9.00 A; B1=1-201.
DR PDB; 4V66; EM; 9.00 A; B1=1-201.
DR PDB; 4V69; EM; 6.70 A; BE=1-201.
DR PDB; 4V6C; X-ray; 3.19 A; BE/DE=1-201.
DR PDB; 4V6D; X-ray; 3.81 A; BE/DE=1-201.
DR PDB; 4V6E; X-ray; 3.71 A; BE/DE=1-201.
DR PDB; 4V6K; EM; 8.25 A; AF=1-201.
DR PDB; 4V6L; EM; 13.20 A; BF=1-201.
DR PDB; 4V6M; EM; 7.10 A; BE=1-201.
DR PDB; 4V6N; EM; 12.10 A; AF=1-201.
DR PDB; 4V6O; EM; 14.70 A; BF=1-201.
DR PDB; 4V6P; EM; 13.50 A; BF=1-201.
DR PDB; 4V6Q; EM; 11.50 A; BF=1-201.
DR PDB; 4V6R; EM; 11.50 A; BF=1-201.
DR PDB; 4V6S; EM; 13.10 A; AF=1-201.
DR PDB; 4V6T; EM; 8.30 A; BE=1-201.
DR PDB; 4V6V; EM; 9.80 A; BF=1-201.
DR PDB; 4V6Y; EM; 12.00 A; BE=1-201.
DR PDB; 4V6Z; EM; 12.00 A; BE=1-201.
DR PDB; 4V70; EM; 17.00 A; BE=1-201.
DR PDB; 4V71; EM; 20.00 A; BE=1-201.
DR PDB; 4V72; EM; 13.00 A; BE=1-201.
DR PDB; 4V73; EM; 15.00 A; BE=1-201.
DR PDB; 4V74; EM; 17.00 A; BE=1-201.
DR PDB; 4V75; EM; 12.00 A; BE=1-201.
DR PDB; 4V76; EM; 17.00 A; BE=1-201.
DR PDB; 4V77; EM; 17.00 A; BE=1-201.
DR PDB; 4V78; EM; 20.00 A; BE=1-201.
DR PDB; 4V79; EM; 15.00 A; BE=1-201.
DR PDB; 4V7A; EM; 9.00 A; BE=1-201.
DR PDB; 4V7B; EM; 6.80 A; BE=1-201.
DR PDB; 4V7C; EM; 7.60 A; BF=1-201.
DR PDB; 4V7D; EM; 7.60 A; AF=1-201.
DR PDB; 4V7I; EM; 9.60 A; AE=1-201.
DR PDB; 4V7S; X-ray; 3.25 A; BE/DE=1-201.
DR PDB; 4V7T; X-ray; 3.19 A; BE/DE=1-201.
DR PDB; 4V7U; X-ray; 3.10 A; BE/DE=1-201.
DR PDB; 4V7V; X-ray; 3.29 A; BE/DE=1-201.
DR PDB; 4V85; X-ray; 3.20 A; BE=1-201.
DR PDB; 4V89; X-ray; 3.70 A; BE=1-201.
DR PDB; 4V9C; X-ray; 3.30 A; BE/DE=1-201.
DR PDB; 4V9D; X-ray; 3.00 A; CE/DE=1-201.
DR PDB; 4V9O; X-ray; 2.90 A; AE/CE/EE/GE=1-201.
DR PDB; 4V9P; X-ray; 2.90 A; AE/CE/EE/GE=1-201.
DR PDB; 4WF1; X-ray; 3.09 A; BE/DE=1-201.
DR PDB; 4WOI; X-ray; 3.00 A; BE/CE=1-201.
DR PDB; 4WWW; X-ray; 3.10 A; RE/YE=1-201.
DR PDB; 4YBB; X-ray; 2.10 A; CE/DE=1-201.
DR PDB; 5ADY; EM; 4.50 A; E=1-201.
DR PDB; 5AFI; EM; 2.90 A; E=1-201.
DR PDB; 5AKA; EM; 5.70 A; E=1-201.
DR PDB; 5GAD; EM; 3.70 A; E=1-201.
DR PDB; 5GAE; EM; 3.33 A; E=1-201.
DR PDB; 5GAF; EM; 4.30 A; E=1-201.
DR PDB; 5GAG; EM; 3.80 A; E=1-201.
DR PDB; 5GAH; EM; 3.80 A; E=1-201.
DR PDB; 5H5U; EM; 3.00 A; E=1-201.
DR PDB; 5IQR; EM; 3.00 A; D=1-201.
DR PDB; 5IT8; X-ray; 3.12 A; CE/DE=1-201.
DR PDB; 5J5B; X-ray; 2.80 A; CE/DE=1-201.
DR PDB; 5J7L; X-ray; 3.00 A; CE/DE=1-201.
DR PDB; 5J88; X-ray; 3.32 A; CE/DE=1-201.
DR PDB; 5J8A; X-ray; 3.10 A; CE/DE=1-201.
DR PDB; 5J91; X-ray; 2.96 A; CE/DE=1-201.
DR PDB; 5JC9; X-ray; 3.03 A; CE/DE=1-201.
DR PDB; 5JTE; EM; 3.60 A; BE=1-201.
DR PDB; 5JU8; EM; 3.60 A; BE=1-201.
DR PDB; 5KCR; EM; 3.60 A; 1F=1-201.
DR PDB; 5KCS; EM; 3.90 A; 1F=1-201.
DR PDB; 5KPS; EM; 3.90 A; D=1-201.
DR PDB; 5KPV; EM; 4.10 A; C=1-201.
DR PDB; 5KPW; EM; 3.90 A; C=1-201.
DR PDB; 5KPX; EM; 3.90 A; C=1-201.
DR PDB; 5L3P; EM; 3.70 A; F=1-201.
DR PDB; 5LZA; EM; 3.60 A; E=1-201.
DR PDB; 5LZB; EM; 5.30 A; E=1-201.
DR PDB; 5LZC; EM; 4.80 A; E=1-201.
DR PDB; 5LZD; EM; 3.40 A; E=1-201.
DR PDB; 5LZE; EM; 3.50 A; E=1-201.
DR PDB; 5LZF; EM; 4.60 A; E=1-201.
DR PDB; 5MDV; EM; 2.97 A; D=1-201.
DR PDB; 5MDW; EM; 3.06 A; D=1-201.
DR PDB; 5MDY; EM; 3.35 A; D=1-201.
DR PDB; 5MDZ; EM; 3.10 A; D=1-201.
DR PDB; 5MGP; EM; 3.10 A; E=1-201.
DR PDB; 5NCO; EM; 4.80 A; E=1-201.
DR PDB; 5NP6; EM; 3.60 A; c=1-201.
DR PDB; 5NWY; EM; 2.93 A; R=1-201.
DR PDB; 5O2R; EM; 3.40 A; E=1-201.
DR PDB; 5U4I; EM; 3.50 A; E=1-201.
DR PDB; 5U9F; EM; 3.20 A; 06=1-201.
DR PDB; 5U9G; EM; 3.20 A; 06=1-201.
DR PDB; 5UYK; EM; 3.90 A; 06=1-201.
DR PDB; 5UYL; EM; 3.60 A; 06=1-201.
DR PDB; 5UYM; EM; 3.20 A; 06=1-201.
DR PDB; 5UYN; EM; 4.00 A; 06=1-201.
DR PDB; 5UYP; EM; 3.90 A; 06=1-201.
DR PDB; 5UYQ; EM; 3.80 A; 06=1-201.
DR PDB; 5WDT; EM; 3.00 A; E=2-201.
DR PDB; 5WE4; EM; 3.10 A; E=2-201.
DR PDB; 5WE6; EM; 3.40 A; E=2-201.
DR PDB; 5WFK; EM; 3.40 A; E=2-201.
DR PDB; 6BU8; EM; 3.50 A; 06=1-201.
DR PDB; 6BY1; X-ray; 3.94 A; CE/DE=21-201.
DR PDB; 6C4I; EM; 3.24 A; E=1-201.
DR PDB; 6ENF; EM; 3.20 A; E=1-201.
DR PDB; 6ENJ; EM; 3.70 A; E=1-201.
DR PDB; 6ENU; EM; 3.10 A; E=1-201.
DR PDB; 6GBZ; EM; 3.80 A; E=1-201.
DR PDB; 6GC0; EM; 3.80 A; E=1-201.
DR PDB; 6GC4; EM; 4.30 A; E=1-201.
DR PDB; 6GC6; EM; 4.30 A; E=1-201.
DR PDB; 6GC7; EM; 4.30 A; E=1-201.
DR PDB; 6GC8; EM; 3.80 A; E=1-201.
DR PDB; 6GWT; EM; 3.80 A; E=1-201.
DR PDB; 6GXM; EM; 3.80 A; E=1-201.
DR PDB; 6GXN; EM; 3.90 A; E=1-201.
DR PDB; 6GXO; EM; 3.90 A; E=1-201.
DR PDB; 6GXP; EM; 4.40 A; E=1-201.
DR PDB; 6H4N; EM; 3.00 A; E=1-201.
DR PDB; 6H58; EM; 7.90 A; E/EE=1-201.
DR PDB; 6HRM; EM; 2.96 A; D=1-201.
DR PDB; 6I0Y; EM; 3.20 A; E=1-201.
DR PDB; 6I7V; X-ray; 2.90 A; CE/DE=1-201.
DR PDB; 6O9J; EM; 3.90 A; E=1-201.
DR PDB; 6O9K; EM; 4.00 A; E=1-201.
DR PDB; 6OFX; EM; 3.30 A; d=1-201.
DR PDB; 6OG7; EM; 3.30 A; d=1-201.
DR PDB; 6ORE; EM; 2.90 A; D=1-201.
DR PDB; 6ORL; EM; 3.50 A; D=1-201.
DR PDB; 6OST; EM; 4.20 A; D=1-201.
DR PDB; 6OT3; EM; 3.90 A; D=1-201.
DR PDB; 6OUO; EM; 3.70 A; D=1-201.
DR PDB; 6PC5; EM; 2.70 A; M=1-201.
DR PDB; 6PC6; EM; 2.50 A; M=1-201.
DR PDB; 6PC7; EM; 2.50 A; M=1-201.
DR PDB; 6PC8; EM; 2.90 A; M=1-201.
DR PDB; 6PCH; EM; 2.90 A; M=1-201.
DR PDB; 6PCQ; EM; 2.60 A; M=1-201.
DR PDB; 6PCR; EM; 2.50 A; M=1-201.
DR PDB; 6PCS; EM; 2.80 A; M=1-201.
DR PDB; 6PCT; EM; 2.80 A; M=1-201.
DR PDB; 6Q97; EM; 3.90 A; D=1-201.
DR PDB; 6Q98; EM; 4.30 A; D=1-201.
DR PDB; 6Q9A; EM; 3.70 A; D=1-201.
DR PDB; 6QDW; EM; 2.83 A; e=1-201.
DR PDB; 6QUL; EM; 3.00 A; E=1-201.
DR PDB; 6S0K; EM; 3.10 A; E=1-201.
DR PDB; 6SZS; EM; 3.06 A; E=1-201.
DR PDB; 6TBV; EM; 2.70 A; L041=1-201.
DR PDB; 6TC3; EM; 2.70 A; L041=1-201.
DR PDB; 6VWL; EM; 3.10 A; C=1-201.
DR PDB; 6VWM; EM; 3.40 A; C=1-201.
DR PDB; 6VWN; EM; 3.40 A; C=1-201.
DR PDB; 6WD6; EM; 3.70 A; d=1-201.
DR PDB; 6WDB; EM; 4.00 A; d=1-201.
DR PDB; 6WDC; EM; 4.20 A; d=1-201.
DR PDB; 6WDD; EM; 3.20 A; d=1-201.
DR PDB; 6WDE; EM; 3.00 A; d=1-201.
DR PDB; 6WDF; EM; 3.30 A; d=1-201.
DR PDB; 6WDG; EM; 3.30 A; d=1-201.
DR PDB; 6WDH; EM; 4.30 A; d=1-201.
DR PDB; 6WDI; EM; 4.00 A; d=1-201.
DR PDB; 6WDJ; EM; 3.70 A; d=1-201.
DR PDB; 6WDK; EM; 3.60 A; d=1-201.
DR PDB; 6WDL; EM; 3.70 A; d=1-201.
DR PDB; 6WDM; EM; 3.60 A; d=1-201.
DR PDB; 6WNT; EM; 3.10 A; d=1-201.
DR PDB; 6WNV; EM; 3.50 A; d=1-201.
DR PDB; 6WNW; EM; 3.20 A; d=1-201.
DR PDB; 6WYV; EM; 2.75 A; M=1-201.
DR PDB; 6XZ7; EM; 2.10 A; E=1-201.
DR PDB; 6XZA; EM; 2.66 A; E2=1-201.
DR PDB; 6XZB; EM; 2.54 A; E2=1-201.
DR PDB; 6Y69; EM; 2.86 A; E=1-201.
DR PDB; 6YS3; EM; 2.58 A; e=1-201.
DR PDB; 6YSR; EM; 3.10 A; E=1-201.
DR PDB; 6YSS; EM; 2.60 A; E=1-201.
DR PDB; 6YST; EM; 3.20 A; E=1-201.
DR PDB; 6YSU; EM; 3.70 A; E=1-201.
DR PDB; 6ZTJ; EM; 3.40 A; BE=1-201.
DR PDB; 6ZTL; EM; 3.50 A; BE=1-201.
DR PDB; 6ZTM; EM; 3.30 A; BE=1-201.
DR PDB; 6ZTN; EM; 3.90 A; BE=1-201.
DR PDB; 6ZTO; EM; 3.00 A; BE=1-201.
DR PDB; 6ZTP; EM; 3.00 A; BE=1-201.
DR PDB; 6ZU1; EM; 3.00 A; BE=1-201.
DR PDB; 7ABZ; EM; 3.21 A; D=1-201.
DR PDB; 7AC7; EM; 3.08 A; D=1-201.
DR PDB; 7ACJ; EM; 3.20 A; D=1-201.
DR PDB; 7ACR; EM; 3.44 A; D=1-201.
DR PDB; 7B5K; EM; 2.90 A; E=1-201.
DR PDB; 7BL2; EM; 3.70 A; E=1-201.
DR PDB; 7BL3; EM; 3.50 A; E=1-201.
DR PDB; 7BL4; EM; 2.40 A; E=1-201.
DR PDB; 7BL5; EM; 3.30 A; E=1-201.
DR PDB; 7BL6; EM; 4.00 A; E=1-201.
DR PDB; 7BV8; EM; 3.14 A; E=1-201.
DR PDB; 7D6Z; EM; 3.40 A; E=1-201.
DR PDB; 7D80; EM; 4.10 A; d=1-201.
DR PDB; 7JSS; EM; 3.70 A; d=1-201.
DR PDB; 7JSW; EM; 3.80 A; d=1-201.
DR PDB; 7JSZ; EM; 3.70 A; d=1-201.
DR PDB; 7JT1; EM; 3.30 A; d=1-201.
DR PDB; 7JT2; EM; 3.50 A; d=1-201.
DR PDB; 7JT3; EM; 3.70 A; d=1-201.
DR PDB; 7K50; EM; 3.40 A; d=1-201.
DR PDB; 7K51; EM; 3.50 A; d=1-201.
DR PDB; 7K52; EM; 3.40 A; d=1-201.
DR PDB; 7K53; EM; 3.20 A; d=1-201.
DR PDB; 7K54; EM; 3.20 A; d=1-201.
DR PDB; 7K55; EM; 3.30 A; d=1-201.
DR PDB; 7LV0; EM; 3.20 A; d=1-201.
DR PDB; 7N1P; EM; 2.33 A; LD=1-201.
DR PDB; 7N2C; EM; 2.72 A; LD=1-201.
DR PDB; 7N2U; EM; 2.53 A; LD=1-201.
DR PDB; 7N2V; EM; 2.54 A; LD=1-201.
DR PDB; 7N30; EM; 2.66 A; LD=1-201.
DR PDB; 7N31; EM; 2.69 A; LD=1-201.
DR PDB; 7NBU; EM; 3.11 A; e=1-201.
DR PDB; 7NSO; EM; 2.90 A; E=1-201.
DR PDB; 7NSP; EM; 3.50 A; E=1-201.
DR PDB; 7NSQ; EM; 3.10 A; E=1-201.
DR PDB; 7NWT; EM; 2.66 A; D=1-201.
DR PDB; 7NWW; EM; 3.05 A; E=1-201.
DR PDB; 7O19; EM; 2.90 A; BE=1-201.
DR PDB; 7O1A; EM; 2.40 A; BE=1-201.
DR PDB; 7O1C; EM; 2.60 A; BE=1-201.
DR PDB; 7OIF; EM; 3.00 A; E=1-201.
DR PDB; 7OIG; EM; 3.20 A; E=1-201.
DR PDB; 7OII; EM; 3.00 A; E=1-201.
DR PDB; 7OIZ; EM; 2.90 A; e=1-201.
DR PDB; 7OJ0; EM; 3.50 A; e=1-201.
DR PDB; 7OT5; EM; 2.90 A; E=1-201.
DR PDB; 7P3K; EM; 2.90 A; e=1-201.
DR PDB; 7PJS; EM; 2.35 A; E=1-201.
DR PDB; 7PJT; EM; 6.00 A; E=1-201.
DR PDB; 7PJV; EM; 3.10 A; E=1-201.
DR PDB; 7PJW; EM; 4.00 A; E=1-201.
DR PDB; 7PJX; EM; 6.50 A; E=1-201.
DR PDB; 7PJY; EM; 3.10 A; E=1-201.
DR PDB; 7PJZ; EM; 6.00 A; E=1-201.
DR PDB; 7QG8; EM; 3.97 A; R=1-201.
DR PDB; 7QGH; EM; 4.48 A; R=1-201.
DR PDB; 7SS9; EM; 3.90 A; d=1-201.
DR PDB; 7SSD; EM; 3.30 A; d=1-201.
DR PDB; 7SSL; EM; 3.80 A; d=1-201.
DR PDB; 7SSN; EM; 3.20 A; d=1-201.
DR PDB; 7SSO; EM; 3.20 A; d=1-201.
DR PDB; 7SSW; EM; 3.80 A; d=1-201.
DR PDB; 7ST2; EM; 2.90 A; d=1-201.
DR PDB; 7ST6; EM; 3.00 A; d=1-201.
DR PDB; 7ST7; EM; 3.20 A; d=1-201.
DR PDBsum; 2J28; -.
DR PDBsum; 2RDO; -.
DR PDBsum; 3BBX; -.
DR PDBsum; 3J5L; -.
DR PDBsum; 3J7Z; -.
DR PDBsum; 3J8G; -.
DR PDBsum; 3J9Y; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 3JBU; -.
DR PDBsum; 3JBV; -.
DR PDBsum; 3JCD; -.
DR PDBsum; 3JCE; -.
DR PDBsum; 3JCJ; -.
DR PDBsum; 3JCN; -.
DR PDBsum; 4CSU; -.
DR PDBsum; 4U1U; -.
DR PDBsum; 4U1V; -.
DR PDBsum; 4U20; -.
DR PDBsum; 4U24; -.
DR PDBsum; 4U25; -.
DR PDBsum; 4U26; -.
DR PDBsum; 4U27; -.
DR PDBsum; 4UY8; -.
DR PDBsum; 4V47; -.
DR PDBsum; 4V48; -.
DR PDBsum; 4V4H; -.
DR PDBsum; 4V4Q; -.
DR PDBsum; 4V4V; -.
DR PDBsum; 4V4W; -.
DR PDBsum; 4V50; -.
DR PDBsum; 4V52; -.
DR PDBsum; 4V53; -.
DR PDBsum; 4V54; -.
DR PDBsum; 4V55; -.
DR PDBsum; 4V56; -.
DR PDBsum; 4V57; -.
DR PDBsum; 4V5B; -.
DR PDBsum; 4V5H; -.
DR PDBsum; 4V5Y; -.
DR PDBsum; 4V64; -.
DR PDBsum; 4V65; -.
DR PDBsum; 4V66; -.
DR PDBsum; 4V69; -.
DR PDBsum; 4V6C; -.
DR PDBsum; 4V6D; -.
DR PDBsum; 4V6E; -.
DR PDBsum; 4V6K; -.
DR PDBsum; 4V6L; -.
DR PDBsum; 4V6M; -.
DR PDBsum; 4V6N; -.
DR PDBsum; 4V6O; -.
DR PDBsum; 4V6P; -.
DR PDBsum; 4V6Q; -.
DR PDBsum; 4V6R; -.
DR PDBsum; 4V6S; -.
DR PDBsum; 4V6T; -.
DR PDBsum; 4V6V; -.
DR PDBsum; 4V6Y; -.
DR PDBsum; 4V6Z; -.
DR PDBsum; 4V70; -.
DR PDBsum; 4V71; -.
DR PDBsum; 4V72; -.
DR PDBsum; 4V73; -.
DR PDBsum; 4V74; -.
DR PDBsum; 4V75; -.
DR PDBsum; 4V76; -.
DR PDBsum; 4V77; -.
DR PDBsum; 4V78; -.
DR PDBsum; 4V79; -.
DR PDBsum; 4V7A; -.
DR PDBsum; 4V7B; -.
DR PDBsum; 4V7C; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V7I; -.
DR PDBsum; 4V7S; -.
DR PDBsum; 4V7T; -.
DR PDBsum; 4V7U; -.
DR PDBsum; 4V7V; -.
DR PDBsum; 4V85; -.
DR PDBsum; 4V89; -.
DR PDBsum; 4V9C; -.
DR PDBsum; 4V9D; -.
DR PDBsum; 4V9O; -.
DR PDBsum; 4V9P; -.
DR PDBsum; 4WF1; -.
DR PDBsum; 4WOI; -.
DR PDBsum; 4WWW; -.
DR PDBsum; 4YBB; -.
DR PDBsum; 5ADY; -.
DR PDBsum; 5AFI; -.
DR PDBsum; 5AKA; -.
DR PDBsum; 5GAD; -.
DR PDBsum; 5GAE; -.
DR PDBsum; 5GAF; -.
DR PDBsum; 5GAG; -.
DR PDBsum; 5GAH; -.
DR PDBsum; 5H5U; -.
DR PDBsum; 5IQR; -.
DR PDBsum; 5IT8; -.
DR PDBsum; 5J5B; -.
DR PDBsum; 5J7L; -.
DR PDBsum; 5J88; -.
DR PDBsum; 5J8A; -.
DR PDBsum; 5J91; -.
DR PDBsum; 5JC9; -.
DR PDBsum; 5JTE; -.
DR PDBsum; 5JU8; -.
DR PDBsum; 5KCR; -.
DR PDBsum; 5KCS; -.
DR PDBsum; 5KPS; -.
DR PDBsum; 5KPV; -.
DR PDBsum; 5KPW; -.
DR PDBsum; 5KPX; -.
DR PDBsum; 5L3P; -.
DR PDBsum; 5LZA; -.
DR PDBsum; 5LZB; -.
DR PDBsum; 5LZC; -.
DR PDBsum; 5LZD; -.
DR PDBsum; 5LZE; -.
DR PDBsum; 5LZF; -.
DR PDBsum; 5MDV; -.
DR PDBsum; 5MDW; -.
DR PDBsum; 5MDY; -.
DR PDBsum; 5MDZ; -.
DR PDBsum; 5MGP; -.
DR PDBsum; 5NCO; -.
DR PDBsum; 5NP6; -.
DR PDBsum; 5NWY; -.
DR PDBsum; 5O2R; -.
DR PDBsum; 5U4I; -.
DR PDBsum; 5U9F; -.
DR PDBsum; 5U9G; -.
DR PDBsum; 5UYK; -.
DR PDBsum; 5UYL; -.
DR PDBsum; 5UYM; -.
DR PDBsum; 5UYN; -.
DR PDBsum; 5UYP; -.
DR PDBsum; 5UYQ; -.
DR PDBsum; 5WDT; -.
DR PDBsum; 5WE4; -.
DR PDBsum; 5WE6; -.
DR PDBsum; 5WFK; -.
DR PDBsum; 6BU8; -.
DR PDBsum; 6BY1; -.
DR PDBsum; 6C4I; -.
DR PDBsum; 6ENF; -.
DR PDBsum; 6ENJ; -.
DR PDBsum; 6ENU; -.
DR PDBsum; 6GBZ; -.
DR PDBsum; 6GC0; -.
DR PDBsum; 6GC4; -.
DR PDBsum; 6GC6; -.
DR PDBsum; 6GC7; -.
DR PDBsum; 6GC8; -.
DR PDBsum; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6I0Y; -.
DR PDBsum; 6I7V; -.
DR PDBsum; 6O9J; -.
DR PDBsum; 6O9K; -.
DR PDBsum; 6OFX; -.
DR PDBsum; 6OG7; -.
DR PDBsum; 6ORE; -.
DR PDBsum; 6ORL; -.
DR PDBsum; 6OST; -.
DR PDBsum; 6OT3; -.
DR PDBsum; 6OUO; -.
DR PDBsum; 6PC5; -.
DR PDBsum; 6PC6; -.
DR PDBsum; 6PC7; -.
DR PDBsum; 6PC8; -.
DR PDBsum; 6PCH; -.
DR PDBsum; 6PCQ; -.
DR PDBsum; 6PCR; -.
DR PDBsum; 6PCS; -.
DR PDBsum; 6PCT; -.
DR PDBsum; 6Q97; -.
DR PDBsum; 6Q98; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6QDW; -.
DR PDBsum; 6QUL; -.
DR PDBsum; 6S0K; -.
DR PDBsum; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6WD6; -.
DR PDBsum; 6WDB; -.
DR PDBsum; 6WDC; -.
DR PDBsum; 6WDD; -.
DR PDBsum; 6WDE; -.
DR PDBsum; 6WDF; -.
DR PDBsum; 6WDG; -.
DR PDBsum; 6WDH; -.
DR PDBsum; 6WDI; -.
DR PDBsum; 6WDJ; -.
DR PDBsum; 6WDK; -.
DR PDBsum; 6WDL; -.
DR PDBsum; 6WDM; -.
DR PDBsum; 6WNT; -.
DR PDBsum; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6WYV; -.
DR PDBsum; 6XZ7; -.
DR PDBsum; 6XZA; -.
DR PDBsum; 6XZB; -.
DR PDBsum; 6Y69; -.
DR PDBsum; 6YS3; -.
DR PDBsum; 6YSR; -.
DR PDBsum; 6YSS; -.
DR PDBsum; 6YST; -.
DR PDBsum; 6YSU; -.
DR PDBsum; 6ZTJ; -.
DR PDBsum; 6ZTL; -.
DR PDBsum; 6ZTM; -.
DR PDBsum; 6ZTN; -.
DR PDBsum; 6ZTO; -.
DR PDBsum; 6ZTP; -.
DR PDBsum; 6ZU1; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7ACJ; -.
DR PDBsum; 7ACR; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BL2; -.
DR PDBsum; 7BL3; -.
DR PDBsum; 7BL4; -.
DR PDBsum; 7BL5; -.
DR PDBsum; 7BL6; -.
DR PDBsum; 7BV8; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7D80; -.
DR PDBsum; 7JSS; -.
DR PDBsum; 7JSW; -.
DR PDBsum; 7JSZ; -.
DR PDBsum; 7JT1; -.
DR PDBsum; 7JT2; -.
DR PDBsum; 7JT3; -.
DR PDBsum; 7K50; -.
DR PDBsum; 7K51; -.
DR PDBsum; 7K52; -.
DR PDBsum; 7K53; -.
DR PDBsum; 7K54; -.
DR PDBsum; 7K55; -.
DR PDBsum; 7LV0; -.
DR PDBsum; 7N1P; -.
DR PDBsum; 7N2C; -.
DR PDBsum; 7N2U; -.
DR PDBsum; 7N2V; -.
DR PDBsum; 7N30; -.
DR PDBsum; 7N31; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7NSO; -.
DR PDBsum; 7NSP; -.
DR PDBsum; 7NSQ; -.
DR PDBsum; 7NWT; -.
DR PDBsum; 7NWW; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7OIF; -.
DR PDBsum; 7OIG; -.
DR PDBsum; 7OII; -.
DR PDBsum; 7OIZ; -.
DR PDBsum; 7OJ0; -.
DR PDBsum; 7OT5; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJS; -.
DR PDBsum; 7PJT; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJW; -.
DR PDBsum; 7PJX; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7PJZ; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7QGH; -.
DR PDBsum; 7SS9; -.
DR PDBsum; 7SSD; -.
DR PDBsum; 7SSL; -.
DR PDBsum; 7SSN; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7SSW; -.
DR PDBsum; 7ST2; -.
DR PDBsum; 7ST6; -.
DR PDBsum; 7ST7; -.
DR AlphaFoldDB; P60723; -.
DR SMR; P60723; -.
DR BioGRID; 4261291; 145.
DR ComplexPortal; CPX-3807; 50S large ribosomal subunit.
DR DIP; DIP-35791N; -.
DR IntAct; P60723; 228.
DR MINT; P60723; -.
DR STRING; 511145.b3319; -.
DR DrugBank; DB13179; Troleandomycin.
DR MoonProt; P60723; -.
DR jPOST; P60723; -.
DR PaxDb; P60723; -.
DR PRIDE; P60723; -.
DR EnsemblBacteria; AAC76344; AAC76344; b3319.
DR EnsemblBacteria; BAE77972; BAE77972; BAE77972.
DR GeneID; 67463983; -.
DR GeneID; 947818; -.
DR KEGG; ecj:JW3281; -.
DR KEGG; eco:b3319; -.
DR PATRIC; fig|1411691.4.peg.3412; -.
DR EchoBASE; EB0860; -.
DR eggNOG; COG0088; Bacteria.
DR HOGENOM; CLU_041575_5_2_6; -.
DR InParanoid; P60723; -.
DR OMA; PQVHILE; -.
DR PhylomeDB; P60723; -.
DR BioCyc; EcoCyc:EG10867-MON; -.
DR BioCyc; MetaCyc:EG10867-MON; -.
DR EvolutionaryTrace; P60723; -.
DR PRO; PR:P60723; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:EcoCyc.
DR GO; GO:0015934; C:large ribosomal subunit; IMP:CAFA.
DR GO; GO:0042788; C:polysomal ribosome; IMP:CAFA.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IDA:EcoCyc.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc.
DR GO; GO:0001070; F:RNA-binding transcription regulator activity; IDA:EcoCyc.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0030371; F:translation repressor activity; IDA:EcoliWiki.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:EcoCyc.
DR GO; GO:0060702; P:negative regulation of endoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CAFA.
DR GO; GO:0017148; P:negative regulation of translation; IMP:CAFA.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0042255; P:ribosome assembly; IMP:CAFA.
DR GO; GO:0031555; P:transcriptional attenuation; IDA:EcoCyc.
DR DisProt; DP00600; -.
DR Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR013005; Ribosomal_uL4/L1e.
DR PANTHER; PTHR10746; PTHR10746; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 1.
DR TIGRFAMs; TIGR03953; rplD_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing;
KW Reference proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Transcription; Transcription regulation;
KW Transcription termination; Translation regulation.
FT CHAIN 1..201
FT /note="50S ribosomal protein L4"
FT /id="PRO_0000129215"
FT REGION 44..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 63
FT /note="K -> E (in strain: N282; confers erythromycin
FT resistance. Ribosomes bind erythromycin poorly and have
FT reduced peptidyltransferase activity. 50S subunits assemble
FT normally, even in the presence of drug, but assembly is
FT cold-sensitive at 20 degrees Celsius)"
FT /evidence="ECO:0000269|PubMed:4589347,
FT ECO:0000269|PubMed:7766155, ECO:0000269|PubMed:7928988"
FT MUTAGEN 40..88
FT /note="Missing: Regulates the S10 operon normally.
FT Assembles into ribosomes in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT MUTAGEN 67..103
FT /note="Missing: Regulates the S10 operon normally. Does not
FT assemble into ribosomes in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT MUTAGEN 93..101
FT /note="Missing: Regulates the S10 operon normally. Not
FT stably associated with the ribosome in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT MUTAGEN 131
FT /note="T->I: Does not regulate the S10 operon; assembles
FT into ribosomes in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT MUTAGEN 134
FT /note="L->P: Does not regulate the S10 operon in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT MUTAGEN 160
FT /note="A->V: Does not regulate the S10 operon; assembles
FT into ribosomes in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT MUTAGEN 167
FT /note="V->D: Does not regulate the S10 operon in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT MUTAGEN 171..201
FT /note="DATGIDPVSLIAFDKVVMTADAVKQVEEMLA->RRSK: Loss of S10
FT operon regulation. Assembles into ribosomes in vivo."
FT /evidence="ECO:0000269|PubMed:8846294"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:6XZ7"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6PC6"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:6XZ7"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:6XZ7"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:6XZ7"
SQ SEQUENCE 201 AA; 22087 MW; 3A953206B0F083B5 CRC64;
MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA EVTGSGKKPW
RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM YRGALKSILS ELVRQDRLIV
VEKFSVEAPK TKLLAQKLKD MALEDVLIIT GELDENLFLA ARNLHKVDVR DATGIDPVSL
IAFDKVVMTA DAVKQVEEML A
