4v56
Crystal structure of the bacterial ribosome from Escherichia coli in complex with spectinomycin.Crystal structure of the bacterial ribosome from Escherichia coli in complex with spectinomycin.
Structural highlights
FunctionRL14_ECOLI This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits. Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8.[1] Can also interact with RsfA, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.[2] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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