Literature DB >> 18607081

Conformational change of the AcrR regulator reveals a possible mechanism of induction.

Ruoyu Gu1, Ming Li, Chih Chia Su, Feng Long, Mathew D Routh, Feng Yang, Gerry McDermott, Edward W Yu.   

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 P222(1) has been reported previously. This P222(1) 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 P3(1) is presented. Comparison of the two AcrR structures reveals possible mechanisms of ligand binding and AcrR regulation.

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Year:  2008        PMID： 18607081      PMCID： PMC2443975          DOI： 10.1107/S1744309108016035

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  26 in total

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Journal:  Antimicrob Agents Chemother       Date:  1992-04       Impact factor: 5.191

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Review 7.  Evolutionary origins of multidrug and drug-specific efflux pumps in bacteria.

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8.  Maximum-likelihood density modification using pattern recognition of structural motifs.

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Authors:  D Ma; M Alberti; C Lynch; H Nikaido; J E Hearst
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10.  Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli.

Authors:  D Ma; D N Cook; M Alberti; N G Pon; H Nikaido; J E Hearst
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  10 in total

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Review 4.  Structures of AcrR and CmeR: insight into the mechanisms of transcriptional repression and multi-drug recognition in the TetR family of regulators.

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8.  The crystal structure of AcrR from Mycobacterium tuberculosis reveals a one-component transcriptional regulation mechanism.

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  10 in total

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