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

Acta Cryst. (2008). F64, 584–588 (doi.org/10.1107/S1744309108016035)

Escherichia coli AcrR represses transcription of acrAB and is induced by many structurally unrelated cytotoxic compounds. The crystal structure of this regulator in space group P222₁ has been reported previously, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. Here, a crystal structure of this regulator in space group P3₁ is presented. A comparison of the two AcrR structures reveals possible mechanisms of ligand binding and AcrR regulation.

R. Gu, M. Li, C.-C. Su, F. Long, M.D. Routh, F. Yang, G. McDermott and E.W. Yu