3q9l
From Proteopedia
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
- ↑ 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
- ↑ 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
