Bactobolin A Binds to a Site on the 70S Ribosome Distinct from Previously Seen Antibiotics

被引：39

作者：

Amunts, Alexey ^{[1
]}

Fiedorczuk, Karol ^{[1
]}

Truong, Thao T. ^{[2
]}

Chandler, Josephine ^{[2
]}

Greenberg, E. Peter ^{[2
]}

Ramakrishnan, V. ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[2] Univ Washington, Sch Med, Dept Microbiol, Seattle, WA 98195 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2015年 / 427卷 / 04期

基金：

英国医学研究理事会; 美国国家科学基金会; 英国惠康基金;

关键词：

translation; antibiotic; P-site; tRNA;

D O I：

10.1016/j.jmb.2014.12.018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ribosome is the target of a large number of antibiotics. Here, we report a 3.4-angstrom-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. (C) 2015 The Authors. Published by Elsevier Ltd.

引用

页码：753 / 755

页数：3

共 6 条

[1] Sources of Diversity in Bactobolin Biosynthesis by Burkholderia thailandensis E264 [J].