4v02: Difference between revisions
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''' | ==MinC:MinD cell division protein complex, Aquifex aeolicus== | ||
<StructureSection load='4v02' size='340' side='right' caption='[[4v02]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4v02]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V02 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4v03|4v03]]</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=4v02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v02 RCSB], [http://www.ebi.ac.uk/pdbsum/4v02 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MINC_AQUAE MINC_AQUAE]] Cell division inhibitor that blocks the formation of 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. Prevents FtsZ polymerization (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
During bacterial cell division, filaments of the tubulin-like protein FtsZ assemble at midcell to form the cytokinetic Z-ring. Its positioning is regulated by the oscillation of MinCDE proteins. MinC is activated by MinD through an unknown mechanism and prevents Z-ring assembly anywhere but midcell. Here, using X-ray crystallography, electron microscopy and in vivo analyses, we show that MinD activates MinC by forming a new class of alternating copolymeric filaments that show similarity to eukaryotic septin filaments. A non-polymerizing mutation in MinD causes aberrant cell division in Escherichia coli. MinCD copolymers bind to membrane, interact with FtsZ and are disassembled by MinE. Imaging a functional msfGFP-MinC fusion protein in MinE-deleted cells reveals filamentous structures. EM imaging of our reconstitution of the MinCD-FtsZ interaction on liposome surfaces reveals a plausible mechanism for regulation of FtsZ ring assembly by MinCD copolymers. | |||
MinCD cell division proteins form alternating copolymeric cytomotive filaments.,Ghosal D, Trambaiolo D, Amos LA, Lowe J Nat Commun. 2014 Dec 15;5:5341. doi: 10.1038/ncomms6341. PMID:25500731<ref>PMID:25500731</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Ghosal, D]] | [[Category: Ghosal, D]] | ||
[[Category: Lowe, J]] | [[Category: Lowe, J]] | ||
[[Category: Bacterial cell division]] | |||
[[Category: Cell cycle]] | |||
[[Category: Ftsz]] | |||
[[Category: Min system]] | |||
Revision as of 13:29, 14 January 2015
MinC:MinD cell division protein complex, Aquifex aeolicus
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