|PROSITE documentation PDOC00505 [for PROSITE entry PS00585]|
Ribosomal protein S5 is one of the proteins from the small ribosomal subunit. In Escherichia coli, S5 is known to be important in the assembly and function of the 30S ribosomal subunit. Mutations in S5 have been shown to increase translational error frequencies.
The crystal structure of the S5 protein has been solved  and consists of two separated domains (see <PDB:1PKP>). An N-terminal domain which displays some structurale homology to the dsRBD domain (α-β(3)-α) (see <PDOC50137>) and a mainly helical C-terminal domain that interacts with S8. The dsRBD domain of the S5 protein interacts with the 16S RNA .
S5 is a protein of 166 to 254 amino-acid residues. The signature pattern for this protein is based on a conserved region, rich in glycine residues located in the N-terminal domain. The profile we developed covers the entire N-terminal dsRBD domain.Last update:
April 2006 / Pattern revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Ramakrishnan V. White S.W.|
|Title||The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA.|
|2||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).|
|3||Authors||All-Robyn J.A. Brown N. Otaka E. Liebman S.W.|
|Source||Mol. Cell. Biol. 10:6544-6553(1990).|
|4||Authors||Otaka E. Hashimoto T. Mizuta K.|
|Source||Protein Seq. Data Anal. 5:285-300(1993).|