2YVE

Crystal structure of the methylene blue-bound form of the multi-drug binding transcriptional repressor CgmR

Summary for 2YVE

• Entry DOI: 10.2210/pdb2yve/pdb
• Related: 2YVH 2zoy 2zoz
• Descriptor: Transcriptional regulator, CHLORIDE ION, 3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM, ... (5 entities in total)
• Functional Keywords: transcriptional regulator, helix-turn-helix, tetr-family, transcription
• Biological source: Corynebacterium glutamicum
• Total number of polymer chains: 2
• Total formula weight: 43869.07

Authors

Itou, H.,Shirakihara, Y.,Tanaka, I. (deposition date: 2007-04-12, release date: 2008-04-15, Last modification date: 2023-10-25)

Primary citation

Itou, H.,Watanabe, N.,Yao, M.,Shirakihara, Y.,Tanaka, I.
Crystal Structures of the Multidrug Binding Repressor Corynebacteriumglutamicum CgmR in Complex with Inducers and with an Operator
J.Mol.Biol., 403:174-184, 2010

PubMed Abstract: CgmR (CGL2612) from Corynebacterium glutamicum is a multidrug-resistance-related transcription factor belonging to the TetR family, which is a protein family of widespread bacterial transcription factors typically involved in environmental response. Here, we report the crystal structures of CgmR homodimeric repressor in complex with two distinct inducers (1.95 and 1.4 Å resolution) and with an operator (2.5 Å resolution). The CgmR-operator complex showed that two CgmR dimers bound to the operator, and each half-site of the palindromic operator was asymmetrically recognized by two DNA-binding domains from different dimers on the opposite sides of the DNA. The inducer complexes demonstrated that both bound inducers act as a wedge to alter the operator-binding conformation of the repressor by steric inhibition. As steric hindrance is used, various drugs should act as inducers if they have sufficient volume for the conformation change and if their bindings sufficiently reduce free energy. The comparative structural study of CgmR free protein, in complex with operator, and with inducers, implies the other mechanism that might contribute to multidrug response of the repressor.

PubMed: 20691702
DOI: 10.1016/j.jmb.2010.07.042

Experimental method

X-RAY DIFFRACTION (1.4 Å)