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| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C0229992 | lld:lifeskim |
| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C1293097 | lld:lifeskim |
| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C0036576 | lld:lifeskim |
| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C0205148 | lld:lifeskim |
| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C1705535 | lld:lifeskim |
| pubmed-article:15458408 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15458408 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15458408 | pubmed:dateCreated | 2004-10-1 | lld:pubmed |
| pubmed-article:15458408 | pubmed:abstractText | Division site selection in Escherichia coli requires that the MinD protein interact with itself and with MinC and MinE. MinD is a member of the NifH-ArsA-Par-MinD subgroup of ATPases. The MinE-MinD interaction results in activation of MinD ATPase activity in the presence of membrane vesicles. The sites within MinD responsible for its interaction with MinC and MinE were studied by site-directed mutagenesis and yeast two-hybrid analysis, guided by the known three-dimensional structure of MinD proteins. This provided evidence that MinC and MinE bind to overlapping sites on the MinD surface. The results also suggested that MinE and the invariant Lys11 residue in the ATPase P-loop of MinD compete for binding to a common site within the MinD structure, thereby providing a plausible structural basis for the ability of MinE to activate the ATPase activity of MinD. | lld:pubmed |
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| pubmed-article:15458408 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15458408 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15458408 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15458408 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15458408 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15458408 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:15458408 | pubmed:author | pubmed-author:KingGlenn FGF | lld:pubmed |
| pubmed-article:15458408 | pubmed:author | pubmed-author:RothfieldLawr... | lld:pubmed |
| pubmed-article:15458408 | pubmed:author | pubmed-author:MaLuyanL | lld:pubmed |
| pubmed-article:15458408 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15458408 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:15458408 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15458408 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15458408 | pubmed:pagination | 99-108 | lld:pubmed |
| pubmed-article:15458408 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15458408 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15458408 | pubmed:articleTitle | Positioning of the MinE binding site on the MinD surface suggests a plausible mechanism for activation of the Escherichia coli MinD ATPase during division site selection. | lld:pubmed |
| pubmed-article:15458408 | pubmed:affiliation | Department of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06032, USA. | lld:pubmed |
| pubmed-article:15458408 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15458408 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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