1Z9C

Crystal structure of OhrR bound to the ohrA promoter: Structure of MarR family protein with operator DNA

1Z9C の概要

• エントリーDOI: 10.2210/pdb1z9c/pdb
• 分子名称: DNA (29-MER), Organic hydroperoxide resistance transcriptional regulator, ... (4 entities in total)
• 機能のキーワード: ohrr, marr family protein, bacterial transcription factor, winged hth protein, transcription-dna complex, transcription/dna
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm: O34777
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 155487.20

構造登録者

Hong, M.,Fuangthong, M.,Helmann, J.D.,Brennan, R.G. (登録日: 2005-04-01, 公開日: 2005-10-25, 最終更新日: 2024-02-14)

主引用文献

Hong, M.,Fuangthong, M.,Helmann, J.D.,Brennan, R.G.
Structure of an OhrR-ohrA Operator Complex Reveals the DNA Binding Mechanism of the MarR Family.
Mol.Cell, 20:131-141, 2005

PubMed Abstract: The mechanisms by which Bacillus subtilis OhrR, a member of the MarR family of transcription regulators, binds the ohrA operator and is induced by oxidation of its lone cysteine residue by organic hydroperoxides to sulphenic acid are unknown. Here, we describe the crystal structures of reduced OhrR and an OhrR-ohrA operator complex. To bind DNA, OhrR employs a chimeric winged helix-turn-helix DNA binding motif, which is composed of extended eukaryotic-like wings, prokaryotic helix-turn-helix motifs, and helix-helix elements. The reactivity of the peroxide-sensing cysteine is not modulated by proximal basic residues but largely by the positive dipole of helix alpha1. Induction originates from the alleviation of intersubunit steric clash between the sulphenic acid moieties of the oxidized sensor cysteines and nearby tyrosines and methionines. The structure of the OhrR-ohrA operator complex reveals the DNA binding mechanism of the entire MarR family and suggests a common inducer binding pocket.

PubMed: 16209951
DOI: 10.1016/j.molcel.2005.09.013

実験手法

X-RAY DIFFRACTION (2.64 Å)