3r9i
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q9l|3q9l]], [[3r9j|3r9j]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q9l|3q9l]], [[3r9j|3r9j]]</td></tr> |
| - | <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> | + | <tr id='gene'><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> |
| - | <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> | + | <tr id='resources'><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> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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> [[http://www.uniprot.org/uniprot/MINE_ECOLI MINE_ECOLI]] Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.<ref>PMID:22380631</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Battaile, K P | + | [[Category: Battaile, K P]] |
| - | [[Category: Holyoak, T | + | [[Category: Holyoak, T]] |
| - | [[Category: Lovell, S | + | [[Category: Lovell, S]] |
| - | [[Category: Lutkenhaus, J | + | [[Category: Lutkenhaus, J]] |
| - | [[Category: Park, K T | + | [[Category: Park, K T]] |
| - | [[Category: Wu, W | + | [[Category: Wu, W]] |
[[Category: Atpase]] | [[Category: Atpase]] | ||
[[Category: Bacterial cell division inhibitor]] | [[Category: Bacterial cell division inhibitor]] | ||
Revision as of 08:26, 25 December 2014
2.6A resolution structure of MinD complexed with MinE (12-31) peptide
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