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Regulation of symmetric bacterial cell division by MinE: What is the role of conformational dynamics?
MedLine Citation:
PMID:  21509194     Owner:  NLM     Status:  PubMed-not-MEDLINE    
Abstract/OtherAbstract:
Symmetric cell division in Gram-negative bacteria requires the concerted action of three Min proteins that together ensure exclusive formation of the cell division septum at the mid-point of the cell. We have recently described the structure and dynamic properties of MinE, the protein responsible for directing the cell division inhibitor complex formed by the MinC and MinD proteins away from the middle of the cell. An unexpected feature of this structure was the location of MinD-binding residues at buried, non-accessible sites in the dimeric interface. Here we elaborate on the potential role of conformational changes that might be involved to allow access to these residues, along with the interesting questions raised by these features of the MinE structure.
Authors:
Houman Ghasriani; Natalie K Goto
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Communicative & integrative biology     Volume:  4     ISSN:  1942-0889     ISO Abbreviation:  Commun Integr Biol     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-04-21     Completed Date:  2011-07-14     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  101478473     Medline TA:  Commun Integr Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  101-3     Citation Subset:  -    
Affiliation:
Department of Chemistry, University of Ottawa; ON Canada.
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