![]() |
|
PROSITE documentation PDOC00556 |
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>) [3]. 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). | |
PubMed ID | 1872840 |
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). | |
PubMed ID | 11866529 | |
DOI | 10.1006/jmbi.2001.5359 |