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| | <StructureSection load='4v02' size='340' side='right'caption='[[4v02]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='4v02' size='340' side='right'caption='[[4v02]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v02]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"aquifex_aeolicus"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001]. 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> | + | <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='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> | + | </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='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'>[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> |
| - | <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://pdbe.org/4v02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v02 RCSB], [http://www.ebi.ac.uk/pdbsum/4v02 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v02 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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). | + | [https://www.uniprot.org/uniprot/O67033_AQUAE O67033_AQUAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquifex aeolicus huber and stetter 2001]] | + | [[Category: Aquifex aeolicus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ghosal, D]] | + | [[Category: Ghosal D]] |
| - | [[Category: Lowe, J]] | + | [[Category: Lowe J]] |
| - | [[Category: Bacterial cell division]]
| + | |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Ftsz]]
| + | |
| - | [[Category: Min system]]
| + | |
| Structural highlights
Function
O67033_AQUAE
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ghosal D, Trambaiolo D, Amos LA, Lowe J. MinCD cell division proteins form alternating copolymeric cytomotive filaments. Nat Commun. 2014 Dec 15;5:5341. doi: 10.1038/ncomms6341. PMID:25500731 doi:http://dx.doi.org/10.1038/ncomms6341
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