spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR001014 Ribosomal protein L23/L25, conserved site

Protein matchesHelp
UniProtKB
Matches:
1224 proteins
AccessionHelp IPR001014 Ribosomal_L23/L25_CS
TypeHelp Conserved_site
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR012677 Nucleotide-binding, alpha-beta plait
IPR012678 Ribosomal protein L23/L15e, core
IPR013025 Ribosomal protein L25/L23
IPR019985 Ribosomal protein L23
GO Term annotationHelp
Process GO:0006412 translation
Function GO:0003723 RNA binding
GO:0003735 structural constituent of ribosome
Component GO:0005622 intracellular
GO:0005840 ribosome
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [1, 2]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.

Many of ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [2, 3].

Ribosomal protein L23 is one of the proteins from the large ribosomal subunit that binds to a specific region on either the 23S or 26S rRNA. This entry includes eukaryotic L25 and bacterial and eukaryotic L23.

Structural linksHelp
PDB - click here
CATH: 3.30.70.330
Database linksHelp
PDBe-motif: PS00050
PROSITE doc: PDOC00049
Blocks: IPB001014

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001014 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P04456 60S ribosomal protein L25

P48162 60S ribosomal protein L23a 1

P61845 50S ribosomal protein L23, chloroplastic

P62750 60S ribosomal protein L23a

P62751 60S ribosomal protein L23a

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001014 Ribosomal protein L23/L25, conserved site
IPR012677 Nucleotide-binding, alpha-beta plait
IPR013025 Ribosomal protein L25/L23
IPR012678 Ribosomal protein L23/L15e, core
IPR019985 Ribosomal protein L23
IPR005633 Ribosomal protein L23/L25, N-terminal
SWISS-MODEL
ModBase

PublicationsHelp
1. Ramakrishnan V, Moore PB.
Atomic structures at last: the ribosome in 2000.
Curr. Opin. Struct. Biol. 11 144-54 2001 [PubMed: 11297922]
http://dx.doi.org/10.1016/S0959-440X(00)00184-6
2. Maguire BA, Zimmermann RA.
The ribosome in focus.
Cell 104 813-6 2001 [PubMed: 11290319]
http://dx.doi.org/10.1016/S0092-8674(01)00278-1
3. Chandra Sanyal S, Liljas A.
The end of the beginning: structural studies of ribosomal proteins.
Curr. Opin. Struct. Biol. 10 633-6 2000 [PubMed: 11114498]
http://dx.doi.org/10.1016/S0959-440X(00)00143-3

Additional ReadingHelp
Ippolito JA, Kanyo ZF, Wang D, Franceschi FJ, Moore PB, Steitz TA, Duffy EM.
Crystal structure of the oxazolidinone antibiotic linezolid bound to the 50S ribosomal subunit.
J. Med. Chem. 51 2008 3353-6 [PubMed: 18494460]
http://dx.doi.org/10.1021/jm800379d
Fearon K, Mason TL.
Structure and function of MRP20 and MRP49, the nuclear genes for two proteins of the 54 S subunit of the yeast mitochondrial ribosome.
J. Biol. Chem. 267 1992 5162-70 [PubMed: 1544898]
http://intl.jbc.org/cgi/reprint/267/8/5162.pdf
Borovinskaya MA, Shoji S, Fredrick K, Cate JH.
Structural basis for hygromycin B inhibition of protein biosynthesis.
RNA 14 2008 1590-9 [PubMed: 18567815]
http://dx.doi.org/10.1261/rna.1076908
Bingel-Erlenmeyer R, Kohler R, Kramer G, Sandikci A, Antolic S, Maier T, Schaffitzel C, Wiedmann B, Bukau B, Ban N.
A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing.
Nature 452 2008 108-11 [PubMed: 18288106]
http://dx.doi.org/10.1038/nature06683
Simonovic M, Steitz TA.
Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNA.
RNA 14 2008 2372-8 [PubMed: 18818369]
http://dx.doi.org/10.1261/rna.1118908
Wilson DN, Schluenzen F, Harms JM, Starosta AL, Connell SR, Fucini P.
The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 13339-44 [PubMed: 18757750]
http://dx.doi.org/10.1073/pnas.0804276105
Raue HA, Otaka E, Suzuki K.
Structural comparison of 26S rRNA-binding ribosomal protein L25 from two different yeast strains and the equivalent proteins from three eubacteria and two chloroplasts.
J. Mol. Evol. 28 1989 418-26 [PubMed: 2501503]
http://dx.doi.org/10.1007/BF02603077
spacer
spacer
InterPro 23.1