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Article
Conformational change of the AcrR regulator reveals a possible mechanism of induction
Acta Crystallographica Section F
  • Ruoyu Gu, Iowa State University
  • Ming Li, Iowa State University
  • Chih-Chia Su, Iowa State University
  • Feng Long, Iowa State University
  • Matthew D. Routh, Iowa State University
  • Feng Yang, Iowa State University
  • Gerry McDermott, University of California - Berkeley
  • Edward Yu, Iowa State University
Document Type
Article
Publication Version
Published Version
Publication Date
1-1-2008
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
Citation Information
Ruoyu Gu, Ming Li, Chih-Chia Su, Feng Long, et al.. "Conformational change of the AcrR regulator reveals a possible mechanism of induction" Acta Crystallographica Section F Vol. 64 Iss. 7 (2008) p. 584 - 588
Available at: http://works.bepress.com/edward_yu/13/