| pubmed-article:11296216 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0007590 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C1947951 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0229992 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0243111 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0599844 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11296216 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:11296216 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:11296216 | pubmed:dateCreated | 2001-4-11 | lld:pubmed |
| pubmed-article:11296216 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296216 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296216 | pubmed:abstractText | Proper placement of the bacterial cell division site requires the site-specific inactivation of other potential division sites. In Escherichia coli, selection of the correct mid-cell site is mediated by the MinC, MinD and MinE proteins. To clarify the functional role of the bacterial cell division inhibitor MinD, which is a membrane-associated ATPase that works as an activator of MinC, we determined the crystal structure of a Pyrococcus furiosus MinD homologue complexed with a substrate analogue, AMPPCP, and with the product ADP at resolutions of 2.7 and 2.0 A, respectively. The structure reveals general similarities to the nitrogenase iron protein, the H-Ras p21 and the RecA-like ATPase domain. Alanine scanning mutational analyses of E.coli MinD were also performed in vivo. The results suggest that the residues around the ATP-binding site are required for the direct interaction with MinC, and that ATP binding and hydrolysis play a role as a molecular switch to control the mechanisms of MinCDE-dependent bacterial cell division. | lld:pubmed |
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| pubmed-article:11296216 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11296216 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296216 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11296216 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296216 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296216 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11296216 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11296216 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11296216 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11296216 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:11296216 | pubmed:author | pubmed-author:OyamaTT | lld:pubmed |
| pubmed-article:11296216 | pubmed:author | pubmed-author:HayashiII | lld:pubmed |
| pubmed-article:11296216 | pubmed:author | pubmed-author:MorikawaKK | lld:pubmed |
| pubmed-article:11296216 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11296216 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:11296216 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:11296216 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11296216 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11296216 | pubmed:pagination | 1819-28 | lld:pubmed |
| pubmed-article:11296216 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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