title: Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus.
abstract: 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.
authors: Department of Structural Biology, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita-City, Osaka 565-0874, Japan.
authors: I
authors: I
authors: Hayashi
authors: T
authors: T
authors: Oyama
authors: K
authors: K
authors: Morikawa
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000235:genetics; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001105:Archaea / Q000166:cytology; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics; D001419:Bacteria / Q000166:cytology; D002455:Cell Division; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D006868:Hydrolysis; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D020027:Pyrococcus furiosus / Q000166:cytology* / Q000201:enzymology*
chemical_list: D019843:Archaeal Proteins; D029968:Escherichia coli Proteins; C005147:5'-adenylyl (beta,gamma-methylene)diphosphonate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C072069:MinD protein, E coli; C002630:alpha,beta-methyleneadenosine 5'-triphosphate