| pubmed-article:16322581 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16322581 | lifeskim:mentions | umls-concept:C0038410 | lld:lifeskim |
| pubmed-article:16322581 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:16322581 | lifeskim:mentions | umls-concept:C1328819 | lld:lifeskim |
| pubmed-article:16322581 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:16322581 | lifeskim:mentions | umls-concept:C0015272 | lld:lifeskim |
| pubmed-article:16322581 | lifeskim:mentions | umls-concept:C1521802 | lld:lifeskim |
| pubmed-article:16322581 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:16322581 | pubmed:dateCreated | 2005-12-2 | lld:pubmed |
| pubmed-article:16322581 | pubmed:abstractText | In a broad genomics analysis to find novel protein targets for antibiotic discovery, MurF was identified as an essential gene product for Streptococcus pneumonia that catalyzes a critical reaction in the biosynthesis of the peptidoglycan in the formation of the cell wall. Lacking close relatives in mammalian biology, MurF presents attractive characteristics as a potential drug target. Initial screening of the Abbott small-molecule compound collection identified several compounds for further validation as pharmaceutical leads. Here we report the integrated efforts of NMR and X-ray crystallography, which reveal the multidomain structure of a MurF-inhibitor complex in a compact conformation that differs dramatically from related structures. The lead molecule is bound in the substrate-binding region and induces domain closure, suggestive of the domain arrangement for the as yet unobserved transition state conformation for MurF enzymes. The results form a basis for directed optimization of the compound lead by structure-based design to explore the suitability of MurF as a pharmaceutical target. | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16322581 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16322581 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16322581 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16322581 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16322581 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:StollVincent... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:LernerClaude... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:BeutelBruce... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:HajdukPhilip... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:JakobClarissa... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:StamperGeoffr... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:GuYu GuiYG | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:EdaljiRohinto... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:SolomonLarry... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:HarlanJohn... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:WalterKarl... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:HolzmanThomas... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:LongeneckerKe... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:FryElizabeth... | lld:pubmed |
| pubmed-article:16322581 | pubmed:author | pubmed-author:BartleyDiane... | lld:pubmed |
| pubmed-article:16322581 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16322581 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:16322581 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16322581 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16322581 | pubmed:pagination | 3039-47 | lld:pubmed |
| pubmed-article:16322581 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
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| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:meshHeading | pubmed-meshheading:16322581... | lld:pubmed |
| pubmed-article:16322581 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16322581 | pubmed:articleTitle | Structure of MurF from Streptococcus pneumoniae co-crystallized with a small molecule inhibitor exhibits interdomain closure. | lld:pubmed |
| pubmed-article:16322581 | pubmed:affiliation | Department of Structural Biology, R46Y, Building AP10, 100 Abbott Park Road, Abbott Park, IL 60064, USA. Kenton.Longenecker@Abbott.com | lld:pubmed |
| pubmed-article:16322581 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:4442412 | entrezgene:pubmed | pubmed-article:16322581 | lld:entrezgene |
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