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

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