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RL23_DEIRA
ID   RL23_DEIRA              Reviewed;          95 AA.
AC   Q9RXK0;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; OrderedLocusNames=DR_0313;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-6, X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S
RP   SUBUNIT, CONTACTS WITH 23S RRNA, AND CONTACTS WITH L29.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=11733066; DOI=10.1016/s0092-8674(01)00546-3;
RA   Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I.,
RA   Bartels H., Franceschi F., Yonath A.;
RT   "High resolution structure of the large ribosomal subunit from a mesophilic
RT   eubacterium.";
RL   Cell 107:679-688(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   FIVE ANTIBIOTICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=11677599; DOI=10.1038/35101544;
RA   Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R.,
RA   Yonath A., Franceschi F.;
RT   "Structural basis for the interaction of antibiotics with the peptidyl
RT   transferase centre in eubacteria.";
RL   Nature 413:814-821(2001).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TRNA MIMICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=12535524; DOI=10.1016/s1097-2765(03)00009-1;
RA   Bashan A., Agmon I., Zarivach R., Schluenzen F., Harms J., Berisio R.,
RA   Bartels H., Franceschi F., Auerbach T., Hansen H.A., Kossoy E., Kessler M.,
RA   Yonath A.;
RT   "Structural basis of the ribosomal machinery for peptide bond formation,
RT   translocation, and nascent chain progression.";
RL   Mol. Cell 11:91-102(2003).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   MODIFIED MACROLIDE ANTIBIOTICS.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=12623020; DOI=10.1016/s0969-2126(03)00022-4;
RA   Schluenzen F., Harms J.M., Franceschi F., Hansen H.A., Bartels H.,
RA   Zarivach R., Yonath A.;
RT   "Structural basis for the antibiotic activity of ketolides and azalides.";
RL   Structure 11:329-338(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TROLEANDOMYCIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=12665853; DOI=10.1038/nsb915;
RA   Berisio R., Schluenzen F., Harms J., Bashan A., Auerbach T., Baram D.,
RA   Yonath A.;
RT   "Structural insight into the role of the ribosomal tunnel in cellular
RT   regulation.";
RL   Nat. Struct. Biol. 10:366-370(2003).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=15059283; DOI=10.1186/1741-7007-2-4;
RA   Harms J.M., Schluenzen F., Fucini P., Bartels H., Yonath A.;
RT   "Alterations at the peptidyl transferase centre of the ribosome induced by
RT   the synergistic action of the streptogramins dalfopristin and
RT   quinupristin.";
RL   BMC Biol. 2:4-4(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TIAMULIN.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=15554968; DOI=10.1111/j.1365-2958.2004.04346.x;
RA   Schluenzen F., Pyetan E., Fucini P., Yonath A., Harms J.M.;
RT   "Inhibition of peptide bond formation by pleuromutilins: the structure of
RT   the 50S ribosomal subunit from Deinococcus radiodurans in complex with
RT   tiamulin.";
RL   Mol. Microbiol. 54:1287-1294(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TRIGGER FACTOR.
RX   PubMed=16091460; DOI=10.1073/pnas.0505581102;
RA   Baram D., Pyetan E., Sittner A., Auerbach-Nevo T., Bashan A., Yonath A.;
RT   "Structure of trigger factor binding domain in biologically homologous
RT   complex with eubacterial ribosome reveals its chaperone action.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12017-12022(2005).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP   TRIGGER FACTOR.
RX   PubMed=16271892; DOI=10.1016/j.str.2005.08.007;
RA   Schluenzen F., Wilson D.N., Tian P., Harms J.M., McInnes S.J.,
RA   Hansen H.A.S., Albrecht R., Buerger J., Wilbanks S.M., Fucini P.;
RT   "The binding mode of the trigger factor on the ribosome: implications for
RT   protein folding and SRP interaction.";
RL   Structure 13:1685-1694(2005).
CC   -!- FUNCTION: One of the early assembly protein (By similarity) it binds
CC       23S rRNA. One of the proteins that surrounds the polypeptide exit
CC       tunnel on the outside of the subunit. Forms the main docking site for
CC       trigger factor binding to the ribosome (PubMed:16091460 and
CC       PubMed:16271892). {ECO:0000250, ECO:0000269|PubMed:16091460,
CC       ECO:0000269|PubMed:16271892}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29 and
CC       trigger factor when it is bound to the ribosome (PubMed:16091460 and
CC       PubMed:16271892). {ECO:0000255|HAMAP-Rule:MF_01369,
CC       ECO:0000269|PubMed:11677599, ECO:0000269|PubMed:12535524,
CC       ECO:0000269|PubMed:12623020, ECO:0000269|PubMed:12665853,
CC       ECO:0000269|PubMed:15059283, ECO:0000269|PubMed:15554968,
CC       ECO:0000269|PubMed:16091460, ECO:0000269|PubMed:16271892}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
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DR   EMBL; AE000513; AAF09894.1; -; Genomic_DNA.
DR   PIR; A75534; A75534.
DR   RefSeq; NP_294036.1; NC_001263.1.
DR   RefSeq; WP_010886958.1; NZ_CP015081.1.
DR   PDB; 1NKW; X-ray; 3.10 A; R=1-95.
DR   PDB; 1NWX; X-ray; 3.50 A; R=2-95.
DR   PDB; 1NWY; X-ray; 3.30 A; R=2-95.
DR   PDB; 1SM1; X-ray; 3.42 A; R=1-95.
DR   PDB; 1XBP; X-ray; 3.50 A; R=2-95.
DR   PDB; 2AAR; X-ray; 3.50 A; R=1-95.
DR   PDB; 2D3O; X-ray; 3.35 A; R=1-95.
DR   PDB; 2ZJP; X-ray; 3.70 A; Q=1-95.
DR   PDB; 2ZJQ; X-ray; 3.30 A; Q=1-95.
DR   PDB; 2ZJR; X-ray; 2.91 A; Q=1-95.
DR   PDB; 3CF5; X-ray; 3.30 A; Q=1-95.
DR   PDB; 3DLL; X-ray; 3.50 A; Q=1-95.
DR   PDB; 3PIO; X-ray; 3.25 A; Q=1-95.
DR   PDB; 3PIP; X-ray; 3.45 A; Q=1-95.
DR   PDB; 4IO9; X-ray; 3.20 A; Q=1-95.
DR   PDB; 4IOA; X-ray; 3.20 A; Q=1-95.
DR   PDB; 4IOC; X-ray; 3.60 A; Q=1-95.
DR   PDB; 4U67; X-ray; 3.65 A; Q=1-95.
DR   PDB; 4V49; X-ray; 8.70 A; R=2-94.
DR   PDB; 4V4A; X-ray; 9.50 A; R=2-94.
DR   PDB; 4V4G; X-ray; 11.50 A; U=2-94.
DR   PDB; 4WFN; X-ray; 3.54 A; Q=1-95.
DR   PDB; 5DM6; X-ray; 2.90 A; Q=2-94.
DR   PDB; 5DM7; X-ray; 3.00 A; Q=2-94.
DR   PDB; 5JVG; X-ray; 3.43 A; Q=1-95.
DR   PDB; 5JVH; X-ray; 3.58 A; Q=1-95.
DR   PDB; 7A0R; X-ray; 3.30 A; Q=2-94.
DR   PDB; 7A0S; X-ray; 3.22 A; Q=2-94.
DR   PDB; 7A18; X-ray; 3.40 A; Q=2-94.
DR   PDBsum; 1NKW; -.
DR   PDBsum; 1NWX; -.
DR   PDBsum; 1NWY; -.
DR   PDBsum; 1SM1; -.
DR   PDBsum; 1XBP; -.
DR   PDBsum; 2AAR; -.
DR   PDBsum; 2D3O; -.
DR   PDBsum; 2ZJP; -.
DR   PDBsum; 2ZJQ; -.
DR   PDBsum; 2ZJR; -.
DR   PDBsum; 3CF5; -.
DR   PDBsum; 3DLL; -.
DR   PDBsum; 3PIO; -.
DR   PDBsum; 3PIP; -.
DR   PDBsum; 4IO9; -.
DR   PDBsum; 4IOA; -.
DR   PDBsum; 4IOC; -.
DR   PDBsum; 4U67; -.
DR   PDBsum; 4V49; -.
DR   PDBsum; 4V4A; -.
DR   PDBsum; 4V4G; -.
DR   PDBsum; 4WFN; -.
DR   PDBsum; 5DM6; -.
DR   PDBsum; 5DM7; -.
DR   PDBsum; 5JVG; -.
DR   PDBsum; 5JVH; -.
DR   PDBsum; 7A0R; -.
DR   PDBsum; 7A0S; -.
DR   PDBsum; 7A18; -.
DR   AlphaFoldDB; Q9RXK0; -.
DR   SMR; Q9RXK0; -.
DR   IntAct; Q9RXK0; 1.
DR   STRING; 243230.DR_0313; -.
DR   EnsemblBacteria; AAF09894; AAF09894; DR_0313.
DR   KEGG; dra:DR_0313; -.
DR   PATRIC; fig|243230.17.peg.479; -.
DR   eggNOG; COG0089; Bacteria.
DR   HOGENOM; CLU_037562_3_1_0; -.
DR   InParanoid; Q9RXK0; -.
DR   OMA; FEVDHRA; -.
DR   OrthoDB; 1978865at2; -.
DR   EvolutionaryTrace; Q9RXK0; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
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:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR   InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   PANTHER; PTHR11620; PTHR11620; 1.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11733066"
FT   CHAIN           2..95
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_0000129406"
FT   HELIX           3..6
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           14..21
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           35..46
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          50..58
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          62..65
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   STRAND          75..83
FT                   /evidence="ECO:0007829|PDB:5DM6"
FT   HELIX           89..92
FT                   /evidence="ECO:0007829|PDB:5DM6"
SQ   SEQUENCE   95 AA;  10522 MW;  09D8AA73699D6046 CRC64;
     MSHYDILQAP VISEKAYSAM ERGVYSFWVS PKATKTEIKD AIQQAFGVRV IGISTMNVPG
     KRKRVGRFIG QRNDRKKAIV RLAEGQSIEA LAGQA
 
 
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