RL24_HALMA
ID RL24_HALMA Reviewed; 120 AA.
AC P10972; Q5V1T4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=50S ribosomal protein L24;
DE AltName: Full=Hl15;
DE AltName: Full=Hl16;
DE AltName: Full=Hmal24;
GN Name=rpl24; OrderedLocusNames=rrnAC1601;
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 [GENOMIC DNA].
RX PubMed=2143141; DOI=10.1016/0014-5793(90)80923-7;
RA Arndt E.;
RT "Nucleotide sequence of four genes encoding ribosomal proteins from the
RT 'S10 and spectinomycin' operon equivalent region in the archaebacterium
RT Halobacterium marismortui.";
RL FEBS Lett. 267:193-198(1990).
RN [2]
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 [3]
RP PROTEIN SEQUENCE OF 2-120.
RX PubMed=3191994; DOI=10.1016/0014-5793(88)80333-8;
RA Hatakeyama T., Hatakeyama T., Kimura M.;
RT "The primary structures of ribosomal proteins L16, L23 and L33 from the
RT archaebacterium Halobacterium marismortui.";
RL FEBS Lett. 240:21-28(1988).
RN [4]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=3196689; DOI=10.1021/bi00418a032;
RA Walsh M.J., McDougall J., Wittmann-Liebold B.;
RT "Extended N-terminal sequencing of proteins of archaebacterial ribosomes
RT blotted from two-dimensional gels onto glass fiber and poly(vinylidene
RT difluoride) membrane.";
RL Biochemistry 27:6867-6876(1988).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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: One of two assembly initiator proteins, it binds directly to
CC the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000250}.
CC -!- FUNCTION: Stabilizes the tertiary rRNA structure within the 23S rRNA
CC domain (domain I) to which it binds. Located at the polypeptide exit
CC tunnel on the outside of the subunit.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with
CC protein L4. {ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X55311; CAA39019.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46518.1; -; Genomic_DNA.
DR PIR; S10735; R5HS24.
DR RefSeq; WP_004957398.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; Q=2-120.
DR PDB; 1JJ2; X-ray; 2.40 A; S=2-120.
DR PDB; 1K73; X-ray; 3.01 A; U=2-120.
DR PDB; 1K8A; X-ray; 3.00 A; U=2-120.
DR PDB; 1K9M; X-ray; 3.00 A; U=2-120.
DR PDB; 1KC8; X-ray; 3.01 A; U=2-120.
DR PDB; 1KD1; X-ray; 3.00 A; U=2-120.
DR PDB; 1KQS; X-ray; 3.10 A; S=2-120.
DR PDB; 1M1K; X-ray; 3.20 A; U=2-120.
DR PDB; 1M90; X-ray; 2.80 A; U=2-120.
DR PDB; 1ML5; EM; 14.00 A; u=2-120.
DR PDB; 1N8R; X-ray; 3.00 A; U=2-120.
DR PDB; 1NJI; X-ray; 3.00 A; U=2-120.
DR PDB; 1Q7Y; X-ray; 3.20 A; U=2-120.
DR PDB; 1Q81; X-ray; 2.95 A; U=2-120.
DR PDB; 1Q82; X-ray; 2.98 A; U=2-120.
DR PDB; 1Q86; X-ray; 3.00 A; U=2-120.
DR PDB; 1QVF; X-ray; 3.10 A; S=2-120.
DR PDB; 1QVG; X-ray; 2.90 A; S=2-120.
DR PDB; 1S72; X-ray; 2.40 A; T=1-120.
DR PDB; 1VQ4; X-ray; 2.70 A; T=1-120.
DR PDB; 1VQ5; X-ray; 2.60 A; T=1-120.
DR PDB; 1VQ6; X-ray; 2.70 A; T=1-120.
DR PDB; 1VQ7; X-ray; 2.50 A; T=1-120.
DR PDB; 1VQ8; X-ray; 2.20 A; T=1-120.
DR PDB; 1VQ9; X-ray; 2.40 A; T=1-120.
DR PDB; 1VQK; X-ray; 2.30 A; T=1-120.
DR PDB; 1VQL; X-ray; 2.30 A; T=1-120.
DR PDB; 1VQM; X-ray; 2.30 A; T=1-120.
DR PDB; 1VQN; X-ray; 2.40 A; T=1-120.
DR PDB; 1VQO; X-ray; 2.20 A; T=1-120.
DR PDB; 1VQP; X-ray; 2.25 A; T=1-120.
DR PDB; 1W2B; X-ray; 3.50 A; S=2-120.
DR PDB; 1YHQ; X-ray; 2.40 A; T=1-120.
DR PDB; 1YI2; X-ray; 2.65 A; T=1-120.
DR PDB; 1YIJ; X-ray; 2.60 A; T=1-120.
DR PDB; 1YIT; X-ray; 2.80 A; T=1-120.
DR PDB; 1YJ9; X-ray; 2.90 A; T=1-120.
DR PDB; 1YJN; X-ray; 3.00 A; T=1-120.
DR PDB; 1YJW; X-ray; 2.90 A; T=1-120.
DR PDB; 2OTJ; X-ray; 2.90 A; T=1-120.
DR PDB; 2OTL; X-ray; 2.70 A; T=1-120.
DR PDB; 2QA4; X-ray; 3.00 A; T=1-120.
DR PDB; 2QEX; X-ray; 2.90 A; T=1-120.
DR PDB; 3CC2; X-ray; 2.40 A; T=1-120.
DR PDB; 3CC4; X-ray; 2.70 A; T=1-120.
DR PDB; 3CC7; X-ray; 2.70 A; T=1-120.
DR PDB; 3CCE; X-ray; 2.75 A; T=1-120.
DR PDB; 3CCJ; X-ray; 2.70 A; T=1-120.
DR PDB; 3CCL; X-ray; 2.90 A; T=1-120.
DR PDB; 3CCM; X-ray; 2.55 A; T=1-120.
DR PDB; 3CCQ; X-ray; 2.90 A; T=1-120.
DR PDB; 3CCR; X-ray; 3.00 A; T=1-120.
DR PDB; 3CCS; X-ray; 2.95 A; T=1-120.
DR PDB; 3CCU; X-ray; 2.80 A; T=1-120.
DR PDB; 3CCV; X-ray; 2.90 A; T=1-120.
DR PDB; 3CD6; X-ray; 2.75 A; T=1-120.
DR PDB; 3CMA; X-ray; 2.80 A; T=1-120.
DR PDB; 3CME; X-ray; 2.95 A; T=1-120.
DR PDB; 3CPW; X-ray; 2.70 A; S=1-120.
DR PDB; 3CXC; X-ray; 3.00 A; S=2-120.
DR PDB; 3G4S; X-ray; 3.20 A; T=2-120.
DR PDB; 3G6E; X-ray; 2.70 A; T=2-120.
DR PDB; 3G71; X-ray; 2.85 A; T=2-120.
DR PDB; 3I55; X-ray; 3.11 A; T=1-120.
DR PDB; 3I56; X-ray; 2.90 A; T=1-120.
DR PDB; 3OW2; X-ray; 2.70 A; S=2-120.
DR PDB; 4ADX; EM; 6.60 A; T=1-120.
DR PDB; 4V42; X-ray; 5.50 A; BU=2-120.
DR PDB; 4V4R; X-ray; 5.90 A; Y=2-120.
DR PDB; 4V4S; X-ray; 6.76 A; BY=2-120.
DR PDB; 4V4T; X-ray; 6.46 A; Y=2-120.
DR PDB; 4V9F; X-ray; 2.40 A; T=1-120.
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; P10972; -.
DR SMR; P10972; -.
DR IntAct; P10972; 3.
DR STRING; 272569.rrnAC1601; -.
DR EnsemblBacteria; AAV46518; AAV46518; rrnAC1601.
DR GeneID; 40152566; -.
DR GeneID; 64821826; -.
DR KEGG; hma:rrnAC1601; -.
DR PATRIC; fig|272569.17.peg.2290; -.
DR eggNOG; arCOG04094; Archaea.
DR HOGENOM; CLU_093240_2_1_2; -.
DR OMA; VRIMRGD; -.
DR EvolutionaryTrace; P10972; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd06089; KOW_RPL26; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR HAMAP; MF_01326_A; Ribosomal_L24_A; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041988; KOW_RPL26/RPL24.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR005756; Ribosomal_L26/L24P_euk/arc.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11143; PTHR11143; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF16906; Ribosomal_L26; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01080; rplX_A_E; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 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:3191994,
FT ECO:0000269|PubMed:3196689"
FT CHAIN 2..120
FT /note="50S ribosomal protein L24"
FT /id="PRO_0000130767"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 21
FT /note="H -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 107..114
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1VQO"
SQ SEQUENCE 120 AA; 13648 MW; BDEEF21DE1587096 CRC64;
MSKQPDKQRK SQRRAPLHER HKQVRATLSA DLREEYGQRN VRVNAGDTVE VLRGDFAGEE
GEVINVDLDK AVIHVEDVTL EKTDGEEVPR PLDTSNVRVT DLDLEDEKRE ARLESEDDSA
