1g3q: Difference between revisions

Revision as of 04:22, 1 July 2008

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File:1g3q.png

Template:STRUCTURE 1g3q

CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MINDCRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND

Template:ABSTRACT PUBMED 11296216

About this StructureAbout this Structure

1G3Q is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus., Hayashi I, Oyama T, Morikawa K, EMBO J. 2001 Apr 17;20(8):1819-28. PMID:11296216

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OCA

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-'''CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND'''
+===CRYSTAL STRUCTURE ANALYSIS OF PYROCOCCUS FURIOSUS CELL DIVISION ATPASE MIND===
-==Overview==
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-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.
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