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http://purl.uniprot.org/citations/16735476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16735476http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16735476http://www.w3.org/2000/01/rdf-schema#comment"Lipoic acid is essential for the activation of a number of protein complexes involved in key metabolic processes. Growth of Mycobacterium tuberculosis relies on a pathway in which the lipoate attachment group is synthesized from an endogenously produced octanoic acid moiety. In patients with multiple-drug-resistant M. tuberculosis, expression of one gene from this pathway, lipB, encoding for octanoyl-[acyl carrier protein]-protein acyltransferase is considerably up-regulated, thus making it a potential target in the search for novel antiinfectives against tuberculosis. Here we present the crystal structure of the M. tuberculosis LipB protein at atomic resolution, showing an unexpected thioether-linked active-site complex with decanoic acid. We provide evidence that the transferase functions as a cysteine/lysine dyad acyltransferase, in which two invariant residues (Lys-142 and Cys-176) are likely to function as acid/base catalysts. Analysis by MS reveals that the LipB catalytic reaction proceeds by means of an internal thioesteracyl intermediate. Structural comparison of LipB with lipoate protein ligase A indicates that, despite conserved structural and sequence active-site features in the two enzymes, 4'-phosphopantetheine-bound octanoic acid recognition is a specific property of LipB."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0510436103"xsd:string
http://purl.uniprot.org/citations/16735476http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0510436103"xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Cronan J.E."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Cronan J.E."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Li X."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Wilmanns M."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Wilmanns M."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Zhao X."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Zhao X."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Ma Q."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Ma Q."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Geerlof A."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Geerlof A."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Eddine A.N."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Eddine A.N."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Kaufmann S.H.E."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/author"Kaufmann S.H.E."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/16735476http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string