3q9l

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[[Image:3q9l.png|left|200px]]
 
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{{STRUCTURE_3q9l| PDB=3q9l | SCENE= }}
{{STRUCTURE_3q9l| PDB=3q9l | SCENE= }}
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===The structure of the dimeric E.coli MinD-ATP complex===
===The structure of the dimeric E.coli MinD-ATP complex===
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{{ABSTRACT_PUBMED_21231967}}
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==Function==
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[[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>
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{{ABSTRACT_PUBMED_21231967}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:21231967</ref><references group="xtra"/>
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<ref group="xtra">PMID:021231967</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Holyoak, T.]]
[[Category: Holyoak, T.]]
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[[Category: Park, K T.]]
[[Category: Park, K T.]]
[[Category: Wu, W.]]
[[Category: Wu, W.]]
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[[Category: Atpase]]
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[[Category: Bacterial cell division inhibitor]]
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[[Category: Cell cycle]]
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[[Category: Hydrolase]]
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[[Category: Minc]]
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[[Category: Mine]]

Revision as of 08:31, 8 May 2013

Template:STRUCTURE 3q9l

Contents

The structure of the dimeric E.coli MinD-ATP complex

Template:ABSTRACT PUBMED 21231967

Function

[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.[1] [2]

About this Structure

3q9l is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Wu W, Park KT, Holyoak T, Lutkenhaus J. Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC. Mol Microbiol. 2011 Jan 14. doi: 10.1111/j.1365-2958.2010.07536.x. PMID:21231967 doi:10.1111/j.1365-2958.2010.07536.x
  1. ↑ de Boer PA, Crossley RE, Hand AR, Rothfield LI. The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site. EMBO J. 1991 Dec;10(13):4371-80. PMID:1836760
  2. ↑ Li G, Young KD. Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol Microbiol. 2012 Apr;84(2):276-95. doi: 10.1111/j.1365-2958.2012.08021.x. Epub, 2012 Mar 8. PMID:22380631 doi:10.1111/j.1365-2958.2012.08021.x

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