NDLI: Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.

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Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.

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Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Blanchard, John S. Roderick, Steven L. Vetting, Matthew W. Yu, Michael
Description	Country affiliation: United States Author Affiliation: Vetting MW ( Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.)
Abstract	Mycothiol is the predominant low-molecular weight thiol produced by actinomycetes, including Mycobacterium tuberculosis. The last reaction in the biosynthetic pathway for mycothiol is catalyzed by mycothiol synthase (MshD), which acetylates the cysteinyl amine of cysteine-glucosamine-inositol (Cys-GlcN-Ins). The crystal structure of MshD was determined in the presence of coenzyme A and acetyl-CoA. MshD consists of two tandem-repeated domains, each exhibiting the Gcn5-related N-acetyltransferase (GNAT) fold. These two domains superimpose with a root-mean-square deviation of 1.7 A over 88 residues, and each was found to bind one molecule of coenzyme, although the binding sites are quite different. The C-terminal domain has a similar active site to many GNAT members in which the acetyl group of the coenzyme is presented to an open active site slot. However, acetyl-CoA bound to the N-terminal domain is buried, and is apparently not positioned to promote acetyl transfer. A modeled substrate complex indicates that Cys-GlcN-Ins would only fill a portion of a negatively charged channel located between the two domains. This is the first structure determined for an enzyme involved in the biosynthesis of mycothiol.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	12
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2003-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetyltransferases Chemistry Mycobacterium Tuberculosis Enzymology Amino Acid Motifs Binding Sites Crystallography, X-ray Cysteine Databases As Topic Disaccharides Glycopeptides Inositol Models, Molecular Multigene Family Plasmids Metabolism Protein Conformation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Pyrazoles Sulfhydryl Compounds Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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