3r9i

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==2.6A resolution structure of MinD complexed with MinE (12-31) peptide==
==2.6A resolution structure of MinD complexed with MinE (12-31) peptide==
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<StructureSection load='3r9i' size='340' side='right' caption='[[3r9i]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='3r9i' size='340' side='right'caption='[[3r9i]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3r9i]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3R9I FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3r9i]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3R9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3R9I FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q9l|3q9l]], [[3r9j|3r9j]]</td></tr>
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<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></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1175, JW1164, minD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3r9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9i OCA], [https://pdbe.org/3r9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3r9i RCSB], [https://www.ebi.ac.uk/pdbsum/3r9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3r9i ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3r9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3r9i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3r9i RCSB], [http://www.ebi.ac.uk/pdbsum/3r9i PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/MIND_ECOLI MIND_ECOLI] ATPase required for the correct placement of the division site. Cell division inhibitors MinC and MinD act in concert to form an inhibitor capable of blocking formation of the polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.<ref>PMID:1836760</ref> <ref>PMID:22380631</ref>
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== Publication Abstract from PubMed ==
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In E. coli, MinD recruits MinE to the membrane, leading to a coupled oscillation required for spatial regulation of the cytokinetic Z ring. How these proteins interact, however, is not clear because the MinD-binding regions of MinE are sequestered within a six-stranded beta sheet and masked by N-terminal helices. minE mutations that restore interaction between some MinD and MinE mutants were isolated. These mutations alter the MinE structure leading to release of the MinD-binding regions and the N-terminal helices that bind the membrane. Crystallization of MinD-MinE complexes revealed a four-stranded beta sheet MinE dimer with the released beta strands (MinD-binding regions) converted to alpha helices bound to MinD dimers. These results identify the MinD-dependent conformational changes in MinE that convert it from a latent to an active form and lead to a model of how MinE persists at the MinD-membrane surface. PAPERFLICK:
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The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis.,Park KT, Wu W, Battaile KP, Lovell S, Holyoak T, Lutkenhaus J Cell. 2011 Aug 5;146(3):396-407. PMID:21816275<ref>PMID:21816275</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Battaile, K P.]]
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[[Category: Large Structures]]
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[[Category: Holyoak, T.]]
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[[Category: Battaile KP]]
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[[Category: Lovell, S.]]
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[[Category: Holyoak T]]
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[[Category: Lutkenhaus, J.]]
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[[Category: Lovell S]]
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[[Category: Park, K T.]]
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[[Category: Lutkenhaus J]]
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[[Category: Wu, W.]]
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[[Category: Park K-T]]
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[[Category: Atpase]]
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[[Category: Wu W]]
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[[Category: Bacterial cell division inhibitor]]
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[[Category: Cell cycle]]
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[[Category: Hydrolase-cell cycle complex]]
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[[Category: Mine]]
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Current revision

2.6A resolution structure of MinD complexed with MinE (12-31) peptide

PDB ID 3r9i

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