RL24E_HALMA
ID RL24E_HALMA Reviewed; 67 AA.
AC P14116; Q5V5M2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=50S ribosomal protein L24e;
DE AltName: Full=Hl21/Hl22;
GN Name=rpl24e; OrderedLocusNames=rrnAC0104;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-67.
RX PubMed=2591382; DOI=10.1111/j.1432-1033.1989.tb15166.x;
RA Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T.;
RT "Primary structures of five ribosomal proteins from the archaebacterium
RT Halobacterium marismortui and their structural relationships to eubacterial
RT and eukaryotic ribosomal proteins.";
RL Eur. J. Biochem. 185:685-693(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937989; DOI=10.1126/science.289.5481.905;
RA Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.;
RT "The complete atomic structure of the large ribosomal subunit at 2.4 A
RT resolution.";
RL Science 289:905-920(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937990; DOI=10.1126/science.289.5481.920;
RA Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.;
RT "The structural basis of ribosome activity in peptide bond synthesis.";
RL Science 289:920-930(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11828326; DOI=10.1038/nsb758;
RA Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K.,
RA Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.;
RT "A pre-translocational intermediate in protein synthesis observed in
RT crystals of enzymatically active 50S subunits.";
RL Nat. Struct. Biol. 9:225-230(2002).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11483524; DOI=10.1093/emboj/20.15.4214;
RA Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "The kink-turn: a new RNA secondary structure motif.";
RL EMBO J. 20:4214-4221(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FOUR MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12150912; DOI=10.1016/s1097-2765(02)00570-1;
RA Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.;
RT "The structures of four macrolide antibiotics bound to the large ribosomal
RT subunit.";
RL Mol. Cell 10:117-128(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12185246; DOI=10.1073/pnas.172404099;
RA Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structural insights into peptide bond formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12860128; DOI=10.1016/s0022-2836(03)00668-5;
RA Hansen J.L., Moore P.B., Steitz T.A.;
RT "Structures of five antibiotics bound at the peptidyl transferase center of
RT the large ribosomal subunit.";
RL J. Mol. Biol. 330:1061-1075(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT
RP E SITE SUBSTRATES.
RX PubMed=14561884; DOI=10.1261/rna.5120503;
RA Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structures of deacylated tRNA mimics bound to the E site of the large
RT ribosomal subunit.";
RL RNA 9:1345-1352(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RX PubMed=23695244; DOI=10.1107/s0907444913004745;
RA Gabdulkhakov A., Nikonov S., Garber M.;
RT "Revisiting the Haloarcula marismortui 50S ribosomal subunit model.";
RL Acta Crystallogr. D 69:997-1004(2013).
CC -!- FUNCTION: Binds to the 23S rRNA.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L3 and L14. {ECO:0000269|PubMed:12150912,
CC ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV45180.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV45180.1; ALT_FRAME; Genomic_DNA.
DR PIR; S06846; R6HS21.
DR PDB; 1FFK; X-ray; 2.40 A; R=2-67.
DR PDB; 1JJ2; X-ray; 2.40 A; T=2-67.
DR PDB; 1K73; X-ray; 3.01 A; V=2-67.
DR PDB; 1K8A; X-ray; 3.00 A; V=2-67.
DR PDB; 1K9M; X-ray; 3.00 A; V=2-67.
DR PDB; 1KC8; X-ray; 3.01 A; V=2-67.
DR PDB; 1KD1; X-ray; 3.00 A; V=2-67.
DR PDB; 1KQS; X-ray; 3.10 A; T=2-67.
DR PDB; 1M1K; X-ray; 3.20 A; V=2-67.
DR PDB; 1M90; X-ray; 2.80 A; V=2-67.
DR PDB; 1ML5; EM; 14.00 A; r=2-67.
DR PDB; 1N8R; X-ray; 3.00 A; V=2-67.
DR PDB; 1NJI; X-ray; 3.00 A; V=2-67.
DR PDB; 1Q7Y; X-ray; 3.20 A; V=2-67.
DR PDB; 1Q81; X-ray; 2.95 A; V=2-67.
DR PDB; 1Q82; X-ray; 2.98 A; V=2-67.
DR PDB; 1Q86; X-ray; 3.00 A; V=2-67.
DR PDB; 1QVF; X-ray; 3.10 A; T=2-67.
DR PDB; 1QVG; X-ray; 2.90 A; T=2-67.
DR PDB; 1S72; X-ray; 2.40 A; U=2-67.
DR PDB; 1VQ4; X-ray; 2.70 A; U=2-67.
DR PDB; 1VQ5; X-ray; 2.60 A; U=2-67.
DR PDB; 1VQ6; X-ray; 2.70 A; U=2-67.
DR PDB; 1VQ7; X-ray; 2.50 A; U=2-67.
DR PDB; 1VQ8; X-ray; 2.20 A; U=2-67.
DR PDB; 1VQ9; X-ray; 2.40 A; U=2-67.
DR PDB; 1VQK; X-ray; 2.30 A; U=2-67.
DR PDB; 1VQL; X-ray; 2.30 A; U=2-67.
DR PDB; 1VQM; X-ray; 2.30 A; U=2-67.
DR PDB; 1VQN; X-ray; 2.40 A; U=2-67.
DR PDB; 1VQO; X-ray; 2.20 A; U=2-67.
DR PDB; 1VQP; X-ray; 2.25 A; U=2-67.
DR PDB; 1W2B; X-ray; 3.50 A; T=2-67.
DR PDB; 1YHQ; X-ray; 2.40 A; U=2-67.
DR PDB; 1YI2; X-ray; 2.65 A; U=2-67.
DR PDB; 1YIJ; X-ray; 2.60 A; U=2-67.
DR PDB; 1YIT; X-ray; 2.80 A; U=2-67.
DR PDB; 1YJ9; X-ray; 2.80 A; U=2-67.
DR PDB; 1YJN; X-ray; 3.00 A; U=2-67.
DR PDB; 1YJW; X-ray; 2.90 A; U=2-67.
DR PDB; 2OTJ; X-ray; 2.90 A; U=2-67.
DR PDB; 2OTL; X-ray; 2.70 A; U=2-67.
DR PDB; 2QA4; X-ray; 3.00 A; U=1-67.
DR PDB; 2QEX; X-ray; 2.90 A; U=1-67.
DR PDB; 3CC2; X-ray; 2.40 A; U=1-67.
DR PDB; 3CC4; X-ray; 2.70 A; U=1-67.
DR PDB; 3CC7; X-ray; 2.70 A; U=1-67.
DR PDB; 3CCE; X-ray; 2.75 A; U=1-67.
DR PDB; 3CCJ; X-ray; 2.70 A; U=1-67.
DR PDB; 3CCL; X-ray; 2.90 A; U=1-67.
DR PDB; 3CCM; X-ray; 2.55 A; U=1-67.
DR PDB; 3CCQ; X-ray; 2.90 A; U=1-67.
DR PDB; 3CCR; X-ray; 3.00 A; U=1-67.
DR PDB; 3CCS; X-ray; 2.95 A; U=1-67.
DR PDB; 3CCU; X-ray; 2.80 A; U=1-67.
DR PDB; 3CCV; X-ray; 2.90 A; U=1-67.
DR PDB; 3CD6; X-ray; 2.75 A; U=1-67.
DR PDB; 3CMA; X-ray; 2.80 A; U=1-67.
DR PDB; 3CME; X-ray; 2.95 A; U=1-67.
DR PDB; 3CPW; X-ray; 2.70 A; T=1-67.
DR PDB; 3CXC; X-ray; 3.00 A; T=2-67.
DR PDB; 3G4S; X-ray; 3.20 A; U=5-57.
DR PDB; 3G6E; X-ray; 2.70 A; U=5-57.
DR PDB; 3G71; X-ray; 2.85 A; U=5-57.
DR PDB; 3I55; X-ray; 3.11 A; U=2-67.
DR PDB; 3I56; X-ray; 2.90 A; U=2-67.
DR PDB; 3OW2; X-ray; 2.70 A; T=5-57.
DR PDB; 4ADX; EM; 6.60 A; U=1-67.
DR PDB; 4V42; X-ray; 5.50 A; BR=2-67.
DR PDB; 4V4R; X-ray; 5.90 A; T=2-67.
DR PDB; 4V4S; X-ray; 6.76 A; T=2-67.
DR PDB; 4V4T; X-ray; 6.46 A; T=2-67.
DR PDB; 4V9F; X-ray; 2.40 A; U=1-67.
DR PDBsum; 1FFK; -.
DR PDBsum; 1JJ2; -.
DR PDBsum; 1K73; -.
DR PDBsum; 1K8A; -.
DR PDBsum; 1K9M; -.
DR PDBsum; 1KC8; -.
DR PDBsum; 1KD1; -.
DR PDBsum; 1KQS; -.
DR PDBsum; 1M1K; -.
DR PDBsum; 1M90; -.
DR PDBsum; 1ML5; -.
DR PDBsum; 1N8R; -.
DR PDBsum; 1NJI; -.
DR PDBsum; 1Q7Y; -.
DR PDBsum; 1Q81; -.
DR PDBsum; 1Q82; -.
DR PDBsum; 1Q86; -.
DR PDBsum; 1QVF; -.
DR PDBsum; 1QVG; -.
DR PDBsum; 1S72; -.
DR PDBsum; 1VQ4; -.
DR PDBsum; 1VQ5; -.
DR PDBsum; 1VQ6; -.
DR PDBsum; 1VQ7; -.
DR PDBsum; 1VQ8; -.
DR PDBsum; 1VQ9; -.
DR PDBsum; 1VQK; -.
DR PDBsum; 1VQL; -.
DR PDBsum; 1VQM; -.
DR PDBsum; 1VQN; -.
DR PDBsum; 1VQO; -.
DR PDBsum; 1VQP; -.
DR PDBsum; 1W2B; -.
DR PDBsum; 1YHQ; -.
DR PDBsum; 1YI2; -.
DR PDBsum; 1YIJ; -.
DR PDBsum; 1YIT; -.
DR PDBsum; 1YJ9; -.
DR PDBsum; 1YJN; -.
DR PDBsum; 1YJW; -.
DR PDBsum; 2OTJ; -.
DR PDBsum; 2OTL; -.
DR PDBsum; 2QA4; -.
DR PDBsum; 2QEX; -.
DR PDBsum; 3CC2; -.
DR PDBsum; 3CC4; -.
DR PDBsum; 3CC7; -.
DR PDBsum; 3CCE; -.
DR PDBsum; 3CCJ; -.
DR PDBsum; 3CCL; -.
DR PDBsum; 3CCM; -.
DR PDBsum; 3CCQ; -.
DR PDBsum; 3CCR; -.
DR PDBsum; 3CCS; -.
DR PDBsum; 3CCU; -.
DR PDBsum; 3CCV; -.
DR PDBsum; 3CD6; -.
DR PDBsum; 3CMA; -.
DR PDBsum; 3CME; -.
DR PDBsum; 3CPW; -.
DR PDBsum; 3CXC; -.
DR PDBsum; 3G4S; -.
DR PDBsum; 3G6E; -.
DR PDBsum; 3G71; -.
DR PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 3OW2; -.
DR PDBsum; 4ADX; -.
DR PDBsum; 4V42; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P14116; -.
DR SMR; P14116; -.
DR IntAct; P14116; 3.
DR STRING; 272569.rrnAC0104; -.
DR EnsemblBacteria; AAV45180; AAV45180; rrnAC0104.
DR KEGG; hma:rrnAC0104; -.
DR PATRIC; fig|272569.17.peg.909; -.
DR eggNOG; arCOG01950; Archaea.
DR HOGENOM; CLU_152994_0_0_2; -.
DR EvolutionaryTrace; P14116; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00472; Ribosomal_L24e_L24; 1.
DR Gene3D; 2.30.170.20; -; 1.
DR HAMAP; MF_00773; Ribosomal_L24e; 1.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR023438; Ribosomal_L24e.
DR InterPro; IPR000988; Ribosomal_L24e-rel.
DR InterPro; IPR023442; Ribosomal_L24e_CS.
DR InterPro; IPR011017; TRASH_dom.
DR Pfam; PF01246; Ribosomal_L24e; 1.
DR SMART; SM00746; TRASH; 1.
DR PROSITE; PS01073; RIBOSOMAL_L24E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2591382"
FT CHAIN 2..67
FT /note="50S ribosomal protein L24e"
FT /id="PRO_0000136913"
FT ZN_FING 7..37
FT /note="C4-type"
FT /evidence="ECO:0000305"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1VQ7"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3CCS"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 67 AA; 7356 MW; D4FCAE00935B7305 CRC64;
MPRTRECDYC GTDIEPGTGT MFVHKDGATT HFCSSKCENN ADLGREARNL EWTDTARGEA
GEAEDEA
