Skip to main content
Journal cover image

Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family.

Publication ,  Journal Article
Hong, M; Fuangthong, M; Helmann, JD; Brennan, RG
Published in: Mol Cell
October 7, 2005

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.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Mol Cell

DOI

ISSN

1097-2765

Publication Date

October 7, 2005

Volume

20

Issue

1

Start / End Page

131 / 141

Location

United States

Related Subject Headings

  • Transcription Factors
  • Repressor Proteins
  • Protein Structure, Tertiary
  • Protein Binding
  • Operator Regions, Genetic
  • Developmental Biology
  • DNA, Bacterial
  • Crystallography, X-Ray
  • Binding Sites
  • Bacterial Proteins
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Hong, M., Fuangthong, M., Helmann, J. D., & Brennan, R. G. (2005). Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol Cell, 20(1), 131–141. https://doi.org/10.1016/j.molcel.2005.09.013
Hong, Minsun, Mayuree Fuangthong, John D. Helmann, and Richard G. Brennan. “Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family.Mol Cell 20, no. 1 (October 7, 2005): 131–41. https://doi.org/10.1016/j.molcel.2005.09.013.
Hong M, Fuangthong M, Helmann JD, Brennan RG. Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol Cell. 2005 Oct 7;20(1):131–41.
Hong, Minsun, et al. “Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family.Mol Cell, vol. 20, no. 1, Oct. 2005, pp. 131–41. Pubmed, doi:10.1016/j.molcel.2005.09.013.
Hong M, Fuangthong M, Helmann JD, Brennan RG. Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol Cell. 2005 Oct 7;20(1):131–141.
Journal cover image

Published In

Mol Cell

DOI

ISSN

1097-2765

Publication Date

October 7, 2005

Volume

20

Issue

1

Start / End Page

131 / 141

Location

United States

Related Subject Headings

  • Transcription Factors
  • Repressor Proteins
  • Protein Structure, Tertiary
  • Protein Binding
  • Operator Regions, Genetic
  • Developmental Biology
  • DNA, Bacterial
  • Crystallography, X-Ray
  • Binding Sites
  • Bacterial Proteins