Assembly and channel opening in a bacterial drug efflux machine

被引：134

作者：

Bavro, Vassiliy N. ^{[1
]}

Pietras, Zbigniew ^{[1
]}

Furnham, Nicholas ^{[1
]}

Perez-Cano, Laura ^{[2
]}

Fernandez-Recio, Juan ^{[2
]}

Pei, Xue Yuan ^{[1
]}

Misra, Rajeev ^{[3
]}

Luisi, Ben ^{[1
]}

机构：

[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England

[2] Barcelona Supercomp Ctr, Dept Life Sci, Barcelona 08034, Spain

[3] Arizona State Univ, Sch Life Sci, Tempe, AZ 85287 USA

来源：

MOLECULAR CELL | 2008年 / 30卷 / 01期

基金：

美国国家卫生研究院; 英国惠康基金;

关键词：

D O I：

10.1016/j.molcel.2008.02.015

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：

Drugs and certain proteins are transported across the membranes of Gram-negative bacteria by energy-activated pumps. The outer membrane component of these pumps is a channel that opens from a sealed resting state during the transport process. We describe two crystal structures of the Escherichia coli outer membrane protein ToIC in its partially open state. Opening is accompanied by the exposure of three shallow intraprotomer grooves in the ToIC trimer, where our mutagenesis data identify a contact point with the periplasmic component of a drug efflux pump, AcrA. We suggest that the assembly of multidrug efflux pumps is accompanied by induced fit of ToIC driven mainly by accommodation of the periplasmic component.

引用

页码：114 / 121

页数：8

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