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Dynamics of the Trimeric AcrB Transporter Protein Inferred From a B-Factor Analysis of the Crystal Structure

Authors
Journal
Proteins Structure Function and Bioinformatics
0887-3585
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
62
Issue
1
Identifiers
DOI: 10.1002/prot.20743
Keywords
  • Article
Disciplines
  • Biology
  • Chemistry

Abstract

The Escherichia coli AcrB multi-drug transporter recognizes a wide range of toxic chemicals and actively extrudes them from cells. The molecular basis of multidrug transport in AcrB remains unknown. Herein, we describe normal mode analyses to study important regions for drug recognition and extrusion in this transporter. Based on the X-ray structure of AcrB, an elastic network model has been able to correct errors arising from crystal imperfection in the experimental B-factors. The results allow us to understand the functional dynamics of this membrane protein. It is expected that this technique can be applied to other membrane proteins with known structures.

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