| pubmed-article:15465043 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15465043 | lifeskim:mentions | umls-concept:C1521802 | lld:lifeskim |
| pubmed-article:15465043 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:15465043 | pubmed:dateCreated | 2004-10-6 | lld:pubmed |
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| pubmed-article:15465043 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:abstractText | Dehydroquinate synthase (DHQS) is a potential target for the development of novel broad-spectrum antimicrobial drugs, active against both prokaryotes and lower eukaryotes. Structures have been reported for Aspergillus nidulans DHQS (AnDHQS) in complexes with a range of ligands. Analysis of these AnDHQS structures showed that a large-scale domain movement occurs during the normal catalytic cycle, with a complex series of structural elements propagating substrate binding-induced conformational changes away from the active site to distal locations. Compared to corresponding fungal enzymes, DHQS from bacterial species are both mono-functional and significantly smaller. We have therefore determined the structure of Staphylococcus aureus DHQS (SaDHQS) in five liganded states, allowing comparison of ligand-induced conformational changes and mechanisms of domain closure between fungal and bacterial enzymes. This comparative analysis shows that substrate binding initiates a large-scale domain closure in both species' DHQS and that the active site stereochemistry, of the catalytically competent closed-form enzyme thus produced, is also highly conserved. However, comparison of AnDHQS and SaDHQS open-form structures, and analysis of the putative dynamic processes by which the transition to the closed-form states are made, shows a far lower degree of similarity, indicating a significant structural divergence. As a result, both the nature of the propagation of conformational change and the mechanical systems involved in this propagation are quite different between the DHQSs from the two species. | lld:pubmed |
| pubmed-article:15465043 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15465043 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15465043 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15465043 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15465043 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:StammersD KDK | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:RecAA | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:NicholsC ECE | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:CharlesII | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:HawkinsA RAR | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:LeslieKK | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:LockyerMM | lld:pubmed |
| pubmed-article:15465043 | pubmed:author | pubmed-author:DhaliwalBB | lld:pubmed |
| pubmed-article:15465043 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15465043 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:15465043 | pubmed:volume | 343 | lld:pubmed |
| pubmed-article:15465043 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15465043 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15465043 | pubmed:pagination | 533-46 | lld:pubmed |
| pubmed-article:15465043 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15465043 | pubmed:meshHeading | pubmed-meshheading:15465043... | lld:pubmed |
| pubmed-article:15465043 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15465043 | pubmed:articleTitle | Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases. | lld:pubmed |
| pubmed-article:15465043 | pubmed:affiliation | Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. | lld:pubmed |
| pubmed-article:15465043 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15465043 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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