Conformational change of the AcrR regulator reveals a possible mechanism of induction
Journal Article
·
· Acta Crystallogr. F
- UCSF
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{sub 1} has been reported previously. This P222{sub 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{sub 1} is presented. Comparison of the two AcrR structures reveals possible mechanisms of ligand binding and AcrR regulation.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1006703
- Journal Information:
- Acta Crystallogr. F, Journal Name: Acta Crystallogr. F Journal Issue: (7) ; 07, 2008 Vol. 64; ISSN 1744-3091
- Country of Publication:
- United States
- Language:
- ENGLISH
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