2QOP

Crystal structure of the transcriptional regulator AcrR from Escherichia coli

Summary for 2QOP

• Entry DOI: 10.2210/pdb2qop/pdb
• Descriptor: HTH-type transcriptional regulator acrR (2 entities in total)
• Functional Keywords: acrb regulator, dna-binding, repressor, transcription, transcription regulation
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 24797.66

Authors

Li, M.,Gu, R.,Su, C.-C.,McDermott, G.,Yu, E.W. (deposition date: 2007-07-20, release date: 2008-02-26, Last modification date: 2024-02-21)

Primary citation

Li, M.,Gu, R.,Su, C.C.,Routh, M.D.,Harris, K.C.,Jewell, E.S.,McDermott, G.,Yu, E.W.
Crystal structure of the transcriptional regulator AcrR from Escherichia coli.
J.Mol.Biol., 374:591-603, 2007

PubMed Abstract: The AcrAB multidrug efflux pump, which belongs to the resistance nodulation division (RND) family, recognizes and extrudes a wide range of antibiotics and chemotherapeutic agents and causes the intrinsic antibiotic resistance in Escherichia coli. The expression of AcrAB is controlled by the transcriptional regulator AcrR, whose open reading frame is located 141 bp upstream of the acrAB operon. To understand the structural basis of AcrR regulation, we have determined the crystal structure of AcrR to 2.55-A resolution, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. Each monomer of AcrR forms a multientrance pocket of 350 A(3) in the ligand-binding domain. The ligand-binding pocket is surrounded with mostly hydrophobic residues. In addition, a completely buried negatively charged glutamate, expected to be critical for drug binding, is located at the center of the binding pocket. The crystal structure provides novel insight into the mechanisms of ligand binding and AcrR regulation.

PubMed: 17950313
DOI: 10.1016/j.jmb.2007.09.064

Experimental method

X-RAY DIFFRACTION (2.55 Å)