1g3q

<table><tr><td colspan='2'>[[1g3q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43587 Atcc 43587]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3Q OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1G3Q FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MIND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1g3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g3q OCA], [http://pdbe.org/1g3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g3q RCSB], [http://www.ebi.ac.uk/pdbsum/1g3q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g3q ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11296216</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 43587]]

[[Category: Hayashi, I]]

[[Category: Morikawa, K]]

[[Category: Oyama, T]]

[[Category: Alpha-beta-alpha layered]]

[[Category: Protein-adp complex]]