Campus Units

Molecular, Cellular and Developmental Biology, Biochemistry, Biophysics and Molecular Biology, Physics and Astronomy

Document Type

Article

Publication Version

Published Version

Publication Date

2008

Journal or Book Title

Acta Crystallographica Section F

Volume

64

Issue

7

First Page

584

Last Page

588

DOI

10.1107/S1744309108016035

Abstract

The Escherichia coli AcrR multidrug-binding protein represses transcription of acrAB and is induced by many structurally unrelated cytotoxic compounds. The crystal structure of AcrR in space group P2221 has been reported previously. This P2221 structure has provided direct information about the multidrug-binding site and important residues for drug recognition. Here, a crystal structure of this regulator in space group P31 is presented. Comparison of the two AcrR structures reveals possible mechanisms of ligand binding and AcrR regulation.

Comments

This article is from Acta Crystallographica Section F 64 (2008): 584, doi:10.1107/S1744309108016035. Posted with permission.

Copyright Owner

International Union of Crystallography

Language

en

File Format

application/pdf

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