RL24_DEIRA
ID RL24_DEIRA Reviewed; 115 AA.
AC Q9RXJ1;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=50S ribosomal protein L24;
GN Name=rplX; OrderedLocusNames=DR_0322;
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 1-5, AND X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE
RP 50S SUBUNIT.
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 (3.35 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 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: One of the proteins that surrounds the polypeptide exit
CC tunnel on the outside of the subunit. Contacts trigger factor (TF) when
CC it is bound to the ribosome; this contact may expose a hydrophobic
CC crevice in TF (PubMed:16271892). {ECO:0000269|PubMed:16271892}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts trigger factor
CC when it is bound to the ribosome (PubMed:16271892).
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:16271892}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF09903.1; -; Genomic_DNA.
DR PIR; B75535; B75535.
DR RefSeq; NP_294045.1; NC_001263.1.
DR RefSeq; WP_010886967.1; NZ_CP015081.1.
DR PDB; 1NKW; X-ray; 3.10 A; S=1-115.
DR PDB; 1NWX; X-ray; 3.50 A; S=1-115.
DR PDB; 1NWY; X-ray; 3.30 A; S=1-115.
DR PDB; 1SM1; X-ray; 3.42 A; S=1-115.
DR PDB; 1XBP; X-ray; 3.50 A; S=1-115.
DR PDB; 2D3O; X-ray; 3.35 A; S=1-115.
DR PDB; 2ZJP; X-ray; 3.70 A; R=1-115.
DR PDB; 2ZJQ; X-ray; 3.30 A; R=1-115.
DR PDB; 2ZJR; X-ray; 2.91 A; R=1-115.
DR PDB; 3CF5; X-ray; 3.30 A; R=1-115.
DR PDB; 3DLL; X-ray; 3.50 A; R=1-115.
DR PDB; 3PIO; X-ray; 3.25 A; R=1-115.
DR PDB; 3PIP; X-ray; 3.45 A; R=1-115.
DR PDB; 4IO9; X-ray; 3.20 A; R=1-115.
DR PDB; 4IOA; X-ray; 3.20 A; R=1-115.
DR PDB; 4IOC; X-ray; 3.60 A; R=1-115.
DR PDB; 4U67; X-ray; 3.65 A; R=2-115.
DR PDB; 4V49; X-ray; 8.70 A; S=2-114.
DR PDB; 4V4A; X-ray; 9.50 A; S=2-114.
DR PDB; 4V4G; X-ray; 11.50 A; V=2-114.
DR PDB; 4WFN; X-ray; 3.54 A; R=1-115.
DR PDB; 5DM6; X-ray; 2.90 A; R=4-113.
DR PDB; 5DM7; X-ray; 3.00 A; R=4-113.
DR PDB; 5JVG; X-ray; 3.43 A; R=1-115.
DR PDB; 5JVH; X-ray; 3.58 A; R=1-115.
DR PDB; 7A0R; X-ray; 3.30 A; R=4-113.
DR PDB; 7A0S; X-ray; 3.22 A; R=4-113.
DR PDB; 7A18; X-ray; 3.40 A; R=4-113.
DR PDBsum; 1NKW; -.
DR PDBsum; 1NWX; -.
DR PDBsum; 1NWY; -.
DR PDBsum; 1SM1; -.
DR PDBsum; 1XBP; -.
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; Q9RXJ1; -.
DR SMR; Q9RXJ1; -.
DR IntAct; Q9RXJ1; 1.
DR STRING; 243230.DR_0322; -.
DR EnsemblBacteria; AAF09903; AAF09903; DR_0322.
DR KEGG; dra:DR_0322; -.
DR PATRIC; fig|243230.17.peg.488; -.
DR eggNOG; COG0198; Bacteria.
DR HOGENOM; CLU_093315_2_3_0; -.
DR InParanoid; Q9RXJ1; -.
DR OMA; HVKPTQE; -.
DR OrthoDB; 2040741at2; -.
DR EvolutionaryTrace; Q9RXJ1; -.
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; IEA:InterPro.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd06089; KOW_RPL26; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041988; KOW_RPL26/RPL24.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR003256; Ribosomal_L24.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR12903; PTHR12903; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF17136; ribosomal_L24; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01079; rplX_bact; 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 CHAIN 1..115
FT /note="50S ribosomal protein L24"
FT /id="PRO_0000130653"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2ZJR"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5DM6"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:5DM6"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5DM6"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2ZJR"
SQ SEQUENCE 115 AA; 12358 MW; FE0A0ABC51477BE1 CRC64;
MPRPSAGSHH NDKLHFKKGD TVIVLSGKHK GQTGKVLLAL PRDQKVVVEG VNVITKNVKP
SMTNPQGGQE QRELALHASK VALVDPETGK ATRVRKQIVD GKKVRVAVAS GKTID
