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

被引：38
|
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：
英国惠康基金; 美国国家科学基金会; 英国医学研究理事会;
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
收藏
页码：753 / 755
页数：3
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