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

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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 Å, 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.