PMID:11296216
| Citation |
Hayashi, I, Oyama, T and Morikawa, K (2001) Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus. EMBO J. 20:1819-28 |
|---|---|
| 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. |
| Links |
PubMed PMC125418 Online version:10.1093/emboj/20.8.1819 |
| Keywords |
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 |
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