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PROSITE documentation PDOC00505 [for PROSITE entry PS50881]

Ribosomal protein S5 signature and profile





Description

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 [1] 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 [2].

S5 belongs to a family of ribosomal proteins which, on the basis of sequence similarities [3,4], groups:

  • Eubacterial S5.
  • Cyanelle S5.
  • Red algal chloroplast S5.
  • Archaebacterial S5.
  • Mammalian S2 (LLrep3).
  • Caenorhabditis elegans S2 (C49H3.11).
  • Drosophila S2.
  • Plant S2.
  • Yeast S4 (SUP44).
  • Fungi mitochondrial S5.

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

S5_DSRBD, PS50881; S5 double stranded RNA-binding domain profile  (MATRIX)

RIBOSOMAL_S5, PS00585; Ribosomal protein S5 signature  (PATTERN)


References

1AuthorsRamakrishnan V. White S.W.
TitleThe structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA.
SourceNature 358:768-771(1992).
PubMed ID1508272
DOI10.1038/358768a0

2AuthorsBrodersen D.E. Clemons W.M. Jr. Carter A.P. Wimberly B.T. Ramakrishnan V.
TitleCrystal structure of the 30 S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 S RNA.
SourceJ. Mol. Biol. 316:725-768(2002).
PubMed ID11866529
DOI10.1006/jmbi.2001.5359

3AuthorsAll-Robyn J.A. Brown N. Otaka E. Liebman S.W.
SourceMol. Cell. Biol. 10:6544-6553(1990).

4AuthorsOtaka E. Hashimoto T. Mizuta K.
SourceProtein Seq. Data Anal. 5:285-300(1993).



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