The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 A resolution

Nat Struct Biol. 2001 Aug;8(8):710-4. doi: 10.1038/90429.


MarR is a regulator of multiple antibiotic resistance in Escherichia coli. It is the prototypical member of the MarR family of regulatory proteins found in bacteria and archaea that play important roles in the development of antibiotic resistance, a global health problem. Here we describe the crystal structure of the MarR protein, determined at a resolution of 2.3 A. This is the first reported crystal structure of a member of this newly-described protein family. The structure shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Dimerization
  • Drug Resistance, Microbial*
  • Drug Resistance, Multiple*
  • Escherichia coli / chemistry*
  • Escherichia coli Proteins*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Subunits
  • Repressor Proteins / chemistry*
  • Repressor Proteins / metabolism
  • Salicylates / metabolism
  • Sequence Alignment


  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • MarR protein, E coli
  • Protein Subunits
  • Repressor Proteins
  • Salicylates

Associated data

  • PDB/1JGS