3BCG

Conformational changes of the AcrR regulator reveal a mechanism of induction

Summary for 3BCG

• Entry DOI: 10.2210/pdb3bcg/pdb
• Descriptor: HTH-type transcriptional regulator acrR (2 entities in total)
• Functional Keywords: acrb regulator, dna-binding, repressor, transcription, transcription regulation, dna binding protein, transcription regulator
• Biological source: Escherichia coli K12
• Total number of polymer chains: 2
• Total formula weight: 49595.32

Authors

Gu, R.,Li, M.,Su, C.C.,Long, F.,Yang, F.,McDermott, G.,Yu, E.Y. (deposition date: 2007-11-12, release date: 2008-02-26, Last modification date: 2024-02-21)

Primary citation

Gu, R.,Li, M.,Su, C.C.,Long, F.,Routh, M.D.,Yang, F.,McDermott, G.,Yu, E.W.
Conformational change of the AcrR regulator reveals a possible mechanism of induction.
Acta Crystallogr.,Sect.F, 64:584-588, 2008

PubMed 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.

PubMed: 18607081
DOI: 10.1107/S1744309108016035

Experimental method

X-RAY DIFFRACTION (2.48 Å)