Publication Date:
2006-09-02
Description:
The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seeger, Markus A -- Schiefner, Andre -- Eicher, Thomas -- Verrey, Francois -- Diederichs, Kay -- Pos, Klaas M -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1295-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Physiology and Zurich Centre for Integrative Human Physiology (ZIHP), University of Zurich, Winterthurerstrasse 190, Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946072" target="_blank"〉PubMed〈/a〉
Keywords:
Biological Transport
;
Crystallization
;
Crystallography, X-Ray
;
Diffusion
;
Drug Resistance, Multiple, Bacterial
;
Escherichia coli/*chemistry/drug effects
;
Escherichia coli Proteins/*chemistry/*metabolism
;
Hydrogen Bonding
;
Hydrophobic and Hydrophilic Interactions
;
Membrane Transport Proteins/*chemistry/metabolism
;
Models, Molecular
;
Multidrug Resistance-Associated Proteins/*chemistry/*metabolism
;
Protein Conformation
;
Protein Structure, Quaternary
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protons
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
