|PROSITE documentation PDOC00556 [for PROSITE entry PS00646]|
Ribosomal protein S13 is one of the proteins from the small ribosomal subunit. In Escherichia coli, S13 is known to be involved in binding fMet-tRNA and, hence, in the initiation of translation. It is a basic protein of 115 to 177 amino-acid residues [1,2].
The crystal structure of the S13 protein has been solved as part of the small ribosomal subunit (see <PDB:1J5E; M>) . It consists of two separated domains, an approximately 60-residue N-terminal domain which forms a small helical domain consisting of two-turn helices and two α-turn structure, and a C-terminal long straight α helix followed by a region devoid of secondary structure. The N-terminal domain makes several base specific interactions with the 16S RNA. Several lysine residues in the C-terminal helix also contact RNA.
Proteins known to belong to this family are listed below.
As a signature pattern, we selected the best conserved regions located at the C-terminal end of the long straight α helix. We also developed a profile which covers the N-terminal domain and the long straight α helix.Last update:
December 2004 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Chan Y.-L., Paz V., Wool I.G.|
|Title||The primary structure of rat ribosomal protein S18.|
|Source||Biochem. Biophys. Res. Commun. 178:1212-1218(1991).|
|2||Authors||Otaka E., Hashimoto T., Mizuta K.|
|Source||Protein Seq. Data Anal. 5:285-300(1993).|
|3||Authors||Brodersen D.E., Clemons W.M. Jr., Carter A.P., Wimberly B.T., Ramakrishnan V.|
|Title||Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 S RNA.|
|Source||J. Mol. Biol. 316:725-768(2002).|