Conformational change of the AcrR regulator reveals a possible mechanism of induction
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2008-01-01
Authors
Gu, Ruoyu
Li, Ming
Su, Chih-Chia
Long, Feng
Routh, Matthew
Yang, Feng
McDermott, Gerry
Yu, Edward
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Yu, Edward
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Physics and Astronomy
Physics and astronomy are basic natural sciences which attempt to describe and provide an understanding of both our world and our universe. Physics serves as the underpinning of many different disciplines including the other natural sciences and technological areas.
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Physics and AstronomyBiochemistry, Biophysics and Molecular BiologyPhysics and Astronomy
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.
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This article is from Acta Crystallographica Section F 64 (2008): 584, doi:10.1107/S1744309108016035. Posted with permission.
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Tue Jan 01 00:00:00 UTC 2008