3BPV

Crystal Structure of MarR

3BPV の概要

• エントリーDOI: 10.2210/pdb3bpv/pdb
• 関連するPDBエントリー: 3BPX
• 分子名称: Transcriptional regulator (2 entities in total)
• 機能のキーワード: marr, dna binding, transcription factor, winged helix motif, dna-binding, transcription regulation, transcription regulator
• 由来する生物種: Methanobacterium thermoautotrophicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16579.30

構造登録者

Saridakis, V.,Shahinas, D.,Xu, X.,Christendat, D. (登録日: 2007-12-19, 公開日: 2008-05-20, 最終更新日: 2024-02-21)

主引用文献

Saridakis, V.,Shahinas, D.,Xu, X.,Christendat, D.
Structural insight on the mechanism of regulation of the MarR family of proteins: high-resolution crystal structure of a transcriptional repressor from Methanobacterium thermoautotrophicum.
J.Mol.Biol., 377:655-667, 2008

PubMed Abstract: Transcriptional regulators belonging to the MarR family are characterized by a winged-helix DNA binding domain. These transcriptional regulators regulate the efflux and influx of phenolic agents in bacteria and archaea. In Escherichia coli, MarR regulates the multiple antibiotic resistance operon and its inactivation produces a multiple antibiotic resistance phenotype. In some organisms, active efflux of drug compounds will produce a drug resistance phenotype, whereas in other organisms, active influx of chlorinated hydrocarbons results in their rapid degradation. Although proteins in the MarR family are regulators of important biological processes, their mechanism of action is not well understood and structural information about how phenolic agents regulate the activity of these proteins is lacking. This article presents the three-dimensional structure of a protein of the MarR family, MTH313, in its apo form and in complex with salicylate, a known inactivator. A comparison of these two structures indicates that the mechanism of regulation involves a large conformational change in the DNA binding lobe. Electrophoretic mobility shift assay and biophysical analyses further suggest that salicylate inactivates MTH313 and prevents it from binding to its promoter region.

PubMed: 18272181
DOI: 10.1016/j.jmb.2008.01.001

実験手法

X-RAY DIFFRACTION (1.4 Å)