Ligand-gated diffusion across the bacterial outer membrane

被引：55

作者：

Lepore, Bryan W. ^{[1
]}

Indic, Mridhu ^{[1
]}

Pham, Hannah ^{[1
]}

Hearn, Elizabeth M. ^{[1
]}

Patel, Dimki R. ^{[1
]}

van den Berg, Bert ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Program Mol Med, Worcester, MA 01605 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2011年 / 108卷 / 25期

基金：

美国国家卫生研究院;

关键词：

CHAIN FATTY-ACIDS; TRANSMEMBRANE PASSAGE; MOLECULAR-BASIS; PROTEIN FADL; TRANSPORT;

D O I：

10.1073/pnas.1018532108

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Ligand-gated channels, in which a substrate transport pathway is formed as a result of the binding of a small-molecule chemical messenger, constitute a diverse class of membrane proteins with important functions in prokaryotic and eukaryotic organisms. Despite their widespread nature, no ligand-gated channels have yet been found within the outer membrane (OM) of Gram-negative bacteria. Here we show, using in vivo transport assays, intrinsic tryptophan fluorescence and X-ray crystallography, that high-affinity (submicromolar) substrate binding to the OM long-chain fatty acid transporter FadL from Escherichia coli causes conformational changes in the N terminus that open up a channel for substrate diffusion. The OM long-chain fatty acid transporter FadL from E. coli is a unique paradigm for OM diffusion-driven transport, in which ligand gating within a beta-barrel membrane protein is a prerequisite for channel formation.

引用

页码：10121 / 10126

页数：6

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