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

共 25 条

[1] PHENIX: a comprehensive Python']Python-based system for macromolecular structure solution [J].

Adams, Paul D. ;

Afonine, Pavel V. ;

Bunkoczi, Gabor ;

Chen, Vincent B. ;

Davis, Ian W. ;

Echols, Nathaniel ;

Headd, Jeffrey J. ;

Hung, Li-Wei ;

Kapral, Gary J. ;

Grosse-Kunstleve, Ralf W. ;

McCoy, Airlie J. ;

Moriarty, Nigel W. ;

Oeffner, Robert ;

Read, Randy J. ;

Richardson, David C. ;

Richardson, Jane S. ;

Terwilliger, Thomas C. ;

Zwart, Peter H. .

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 2010, 66 :213-221

[2]

[Anonymous], PYMOL MOL GRAPH SYST

[3] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].

BAILEY, S .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1994, 50 :760-763

[4] EVIDENCE THAT HIS(110) OF THE PROTEIN FADL IN THE OUTER-MEMBRANE OF ESCHERICHIA-COLI IS INVOLVED IN THE BINDING AND UPTAKE OF LONG-CHAIN FATTY-ACIDS - POSSIBLE ROLE OF THIS RESIDUE IN CARBOXYLATE BINDING [J].

BLACK, PN ;

ZHANG, Q .

BIOCHEMICAL JOURNAL, 1995, 310 :389-394

[5] Version 1.2 of the Crystallography and NMR system [J].

Brunger, Axel T. .

NATURE PROTOCOLS, 2007, 2 (11) :2728-2733

[6] Molecular basis of the CRAC channel [J].

Cahalan, Michael D. ;

Zhang, Shenyuan L. ;

Yeromin, Andriy V. ;

Ohlsen, Kari ;

Roos, Jack ;

Stauderman, Kenneth A. .

CELL CALCIUM, 2007, 42 (02) :133-144

[7]

Copeland R.A., 2000, ENZYMES PRACTICAL IN, Vsecond, P94

[8] Features and development of Coot [J].

Emsley, P. ;

Lohkamp, B. ;

Scott, W. G. ;

Cowtan, K. .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2010, 66 :486-501

[9] TonB-dependent receptors - structural perspectives [J].

Ferguson, AD ;

Deisenhofer, J .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2002, 1565 (02) :318-332

[10] TIGHT REGULATION, MODULATION, AND HIGH-LEVEL EXPRESSION BY VECTORS CONTAINING THE ARABINOSE P-BAD PROMOTER [J].

GUZMAN, LM ;

BELIN, D ;

CARSON, MJ ;

BECKWITH, J .

JOURNAL OF BACTERIOLOGY, 1995, 177 (14) :4121-4130

← 1 2 3 →