Structural highlights
4v57 is a 20 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entries 2qoy, 2qoz, 2qp0 and 2qp1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Method: | X-ray diffraction, Resolution 3.5Å |
Ligands: | , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
RS8_ECOLI One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit (By similarity).[HAMAP-Rule:MF_01302_B] Protein S8 is a translational repressor protein, it controls the translation of the spc operon by binding to its mRNA.[HAMAP-Rule:MF_01302_B]
Publication Abstract from PubMed
The widely used antibiotic spectinomycin inhibits bacterial protein synthesis by blocking translocation of messenger RNA and transfer RNAs on the ribosome. Here, we show that in crystals of the Escherichia coli 70S ribosome spectinomycin binding traps a distinct swiveling state of the head domain of the small ribosomal subunit. Spectinomycin also alters the rate and completeness of reverse translocation in vitro. These structural and biochemical data indicate that in solution spectinomycin sterically blocks swiveling of the head domain of the small ribosomal subunit and thereby disrupts the translocation cycle.
A steric block in translation caused by the antibiotic spectinomycin.,Borovinskaya MA, Shoji S, Holton JM, Fredrick K, Cate JH ACS Chem Biol. 2007 Aug 17;2(8):545-52. Epub 2007 Aug 10. PMID:17696316[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Borovinskaya MA, Shoji S, Holton JM, Fredrick K, Cate JH. A steric block in translation caused by the antibiotic spectinomycin. ACS Chem Biol. 2007 Aug 17;2(8):545-52. Epub 2007 Aug 10. PMID:17696316 doi:http://dx.doi.org/10.1021/cb700100n