View source for 4v02


==MinC:MinD cell division protein complex, Aquifex aeolicus==
<StructureSection load='4v02' size='340' side='right'caption='[[4v02]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4v02]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4V02 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4v02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v02 OCA], [https://pdbe.org/4v02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v02 RCSB], [https://www.ebi.ac.uk/pdbsum/4v02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v02 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O67033_AQUAE O67033_AQUAE] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4v02" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Large Structures]]
[[Category: Ghosal D]]
[[Category: Lowe J]]