Summary
Escherichia coli, the cell division site is determined by the cooperative activity of min operon products MinC, MinD, and MinE. MinC is a nonspecific inhibitor of the septum protein FtsZ, and MinE is the supressor of MinC. MinD plays a multifunctional role. It is a membrane-associated ATPase and is a septum site-determining factor through the activation and regulation of MinC and MinE. MinD is also known to undergo a rapid pole-to-pole oscillation movement in vivo as observed by fluorescent microscopy. The three-dimensional structure of the MinD-2 from Pyrococcus horikoshii OT3 (PH0612) has been determined at 2.3 A resolution by X-ray crystallography using the Se-Met MAD method. The molecule consists of a {beta}-sheet with seven parallel and one antiparallel strands and eleven peripheral {alpha}-helices. It contains the classical mononucleotide-binding loop with bound ADP and magnesium ion, which is consistent with the suggested ATPase activity. Structure analysis shows that MinD is most similar to nitrogenase iron protein which is a member of the family of the P-loop containing nucleotide triphosphate hydrolase superfamily of proteins.
Figure
Ribbon diagram of the MinD-2 from Pyrococcus horikoshii. The molecule consists of an eight-stranded {beta}-sheet and eleven peripheral {alpha}-helices. Bound ADP (ball and stick) and magnesium ion (gray ball) are also shown.
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