Bactobolin A binds to a site on the 70S ribosome distinct from previously seen antibiotics.
J Mol Biol, 2015/02/27;427(4):753-755.
Amunts A[1], Fiedorczuk K[1], Truong TT[2], Chandler J[2], Greenberg EP[2], Ramakrishnan V[3]
Affiliations
PMID: 25562208DOI: 10.1016/j.jmb.2014.12.018
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Abstract
The ribosome is the target of a large number of antibiotics. Here, we report a 3.4-Å-resolution crystal structure of bactobolin A bound to 70S ribosome-tRNA complex. The antibiotic binds at a previously unseen site in the 50S subunit and displaces tRNA bound at the P-site. It thus likely has a similar mechanism of action as blasticidin S despite binding to a different site. The structure also rationalizes previously identified resistance mutations.
Keywords: P-site; antibiotic; tRNA; translation
MeSH terms
Anti-Bacterial Agents; Benzopyrans; Burkholderia; Crystallography, X-Ray; Multiprotein Complexes; Nucleosides; RNA, Transfer; Ribosome Subunits, Large, Bacterial; Thermus thermophilus
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