The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis

Acta Cryst. (2009). F65, 204-209 [doi.org/10.1107/S174430910900414X]

Members of the multi-antibiotic resistance repressor (MarR) family of transcription factors have been implicated in the control of multi-drug resistance in bacteria. These proteins regulate expression of transporter proteins by binding to specific sites in their gene promoters. We have solved the structure of the MarR protein NMB 1585 from the human pathogen Neisseria meninigitidis. The structure resembles other MarR proteins comprising two wing-like DNA binding domains connected to extended α-helical arms which associate to form the protein dimer.

C.E. Nichols, S. Sainsbury, J. Ren, T.S. Walter, A. Verma, D.K. Stammers, N.J. Saunders and R.J. Owens