1ion
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THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3
OverviewOverview
BACKGROUND: In 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. RESULTS: 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 7 parallel and 1 antiparallel, strands and 11 peripheral alpha helices. It contains the classical, mononucleotide binding loop with bound ADP and magnesium ion, which is, consistent with the suggested ATPase activity. CONCLUSIONS: Structure, analysis shows that MinD is most similar to nitrogenase iron protein, which is a member of the P loop-containing nucleotide triphosphate, hydrolase superfamily of proteins. Unlike nitrogenase or other member, proteins that normally work as a dimer, MinD was present as a monomer in, the crystal. Both the 31P NMR and Malachite Green method exhibited, relatively low levels of ATPase activity. These facts suggest that MinD, may work as a molecular switch in the multiprotein complex in bacterial, cell division.
About this StructureAbout this Structure
1ION is a Single protein structure of sequence from Pyrococcus horikoshii with MG and ADP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of septum site-determining protein MinD from Pyrococcus horikoshii OT3 in complex with Mg-ADP., Sakai N, Yao M, Itou H, Watanabe N, Yumoto F, Tanokura M, Tanaka I, Structure. 2001 Sep;9(9):817-26. PMID:11566131
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