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http://purl.uniprot.org/citations/12958317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12958317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12958317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/12958317http://www.w3.org/2000/01/rdf-schema#comment"Mycothiol (1-D-myo-inosityl 2-(N-acetyl-L-cysteinyl)amido-2-deoxy-alpha-D-glucopyranoside, MSH or AcCys-GlcN-inositol (Ins)) is the major reducing agent in actinomycetes, including Mycobacterium tuberculosis. The biosynthesis of MSH involves a deacetylase that removes the acetyl group from the precursor GlcNAc-Ins to yield GlcN-Ins. The deacetylase (MshB) corresponds to Rv1170 of M. tuberculosis with a molecular mass of 33,400 Da. MshB is a Zn2+ metalloprotein, and the deacetylase activity is completely dependent on the presence of a divalent metal cation. We have determined the x-ray crystallographic structure of MshB, which reveals a protein that folds in a manner resembling lactate dehydrogenase in the N-terminal domain and a C-terminal domain consisting of two beta-sheets and two alpha-helices. The zinc binding site is in the N-terminal domain occupying a position equivalent to that of the NAD+ co-factor of lactate dehydrogenase. The Zn2+ is 5 coordinate with 3 residues from MshB (His-13, Asp-16, His-147) and two water molecules. One water would be displaced upon binding of substrate (GlcNAc-Ins); the other is proposed as the nucleophilic water assisted by the general base carboxylate of Asp-15. In addition to the Zn2+ providing electrophilic assistance in the hydrolysis, His-144 imidazole could form a hydrogen bond to the oxyanion of the tetrahedral intermediate. The extensive sequence identity of MshB, the deacetylase, with mycothiol S-conjugate amidase, an amide hydrolase that mediates detoxification of mycothiol S-conjugate xenobiotics, has allowed us to construct a faithful model of the catalytic domain of mycothiol S-conjugate amidase based on the structure of MshB."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m308914200"xsd:string
http://purl.uniprot.org/citations/12958317http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m308914200"xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Cherney M.M."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Cherney M.M."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"James M.N.G."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"James M.N.G."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Garen C."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Garen C."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Av-Gay Y."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Av-Gay Y."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Fahey R.C."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Fahey R.C."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Newton G."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Newton G."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Maynes J.T."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Maynes J.T."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Arad D."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/author"Arad D."xsd:string
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12958317http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string