Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus

EMBO J. 2001 Apr 17;20(8):1819-28. doi: 10.1093/emboj/20.8.1819.


Proper placement of the bacterial cell division site requires the site-specific inactivation of other potential division sites. In Escherichia coli, selection of the correct mid-cell site is mediated by the MinC, MinD and MinE proteins. To clarify the functional role of the bacterial cell division inhibitor MinD, which is a membrane-associated ATPase that works as an activator of MinC, we determined the crystal structure of a Pyrococcus furiosus MinD homologue complexed with a substrate analogue, AMPPCP, and with the product ADP at resolutions of 2.7 and 2.0 A, respectively. The structure reveals general similarities to the nitrogenase iron protein, the H-Ras p21 and the RecA-like ATPase domain. Alanine scanning mutational analyses of E.coli MinD were also performed in vivo. The results suggest that the residues around the ATP-binding site are required for the direct interaction with MinC, and that ATP binding and hydrolysis play a role as a molecular switch to control the mechanisms of MinCDE-dependent bacterial cell division.

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphate / analogs & derivatives*
  • Adenosine Triphosphate / chemistry*
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Archaea / cytology
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Bacteria / cytology
  • Cell Division
  • Conserved Sequence
  • Crystallography, X-Ray
  • Escherichia coli Proteins*
  • Hydrolysis
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Pyrococcus furiosus / cytology*
  • Pyrococcus furiosus / enzymology*


  • Archaeal Proteins
  • Escherichia coli Proteins
  • 5'-adenylyl (beta,gamma-methylene)diphosphonate
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • MinD protein, E coli
  • alpha,beta-methyleneadenosine 5'-triphosphate

Associated data

  • PDB/1G3Q
  • PDB/1G3R