1ion
From Proteopedia
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'''THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3''' | '''THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3''' | ||
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[[Category: Yao, M.]] | [[Category: Yao, M.]] | ||
[[Category: Yumoto, F.]] | [[Category: Yumoto, F.]] | ||
| - | [[Category: | + | [[Category: Adp-binding protein]] |
| - | [[Category: | + | [[Category: Cell division inhibitor]] |
| - | [[Category: | + | [[Category: Mind]] |
| - | [[Category: | + | [[Category: P-loop]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:13:38 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:13, 2 May 2008
THE SEPTUM SITE-DETERMINING PROTEIN MIND COMPLEXED WITH MG-ADP FROM PYROCOCCUS HORIKOSHII OT3
Overview
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 Structure
1ION is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 20:13:38 2008
