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http://purl.uniprot.org/citations/18420147http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18420147http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18420147http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/18420147http://www.w3.org/2000/01/rdf-schema#comment"Mycobacterium tuberculosis FabH initiates type II fatty acid synthase-catalyzed formation of the long chain (C(16)-C(22)) acyl-coenzyme A (CoA) precursors of mycolic acids, which are major constituents of the bacterial cell envelope. Crystal structures of M. tuberculosis FabH (mtFabH) show the substrate binding site to be a buried, extended L-shaped channel with only a single solvent access portal. Entrance of an acyl-CoA substrate through the solvent portal would require energetically unfavorable reptational threading of the substrate to its reactive position. Using a class of FabH inhibitors, we have tested an alternative hypothesis that FabH exists in an "open" form during substrate binding and product release, and a "closed" form in which catalysis and intermediate steps occur. This hypothesis is supported by mass spectrometric analysis of the product profile and crystal structures of complexes of mtFabH with these inhibitors."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2008.03.007"xsd:string
http://purl.uniprot.org/citations/18420147http://purl.org/dc/terms/identifier"doi:10.1016/j.chembiol.2008.03.007"xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Musayev F.N."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Musayev F.N."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Scarsdale J.N."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Scarsdale J.N."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Reynolds K.A."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Reynolds K.A."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Wright H.T."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Wright H.T."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Sachdeva S."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Sachdeva S."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Alhamadsheh M.M."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/author"Alhamadsheh M.M."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/name"Chem. Biol."xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/pages"402-412"xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/pages"402-412"xsd:string
http://purl.uniprot.org/citations/18420147http://purl.uniprot.org/core/title"Separate entrance and exit portals for ligand traffic in Mycobacterium tuberculosis FabH."xsd:string