HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 283, Issue 23, 15834-15844, June 6, 2008

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 283/23/15834    most recent M801017200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vetting, M. W. Articles by Blanchard, J. S. Search for Related Content PubMed PubMed Citation Articles by Vetting, M. W. Articles by Blanchard, J. S. Social Bookmarking                      What's this?

Structural and Enzymatic Analysis of MshA from Corynebacterium glutamicum

SUBSTRATE-ASSISTED CATALYSIS^*

From the Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461

The glycosyltransferase termed MshA catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to 1-L-myo-inositol-1-phosphate in the first committed step of mycothiol biosynthesis. The structure of MshA from Corynebacterium glutamicum was determined both in the absence of substrates and in a complex with UDP and 1-L-myo-inositol-1-phosphate. MshA belongs to the GT-B structural family whose members have a two-domain structure with both domains exhibiting a Rossman-type fold. Binding of the donor sugar to the C-terminal domain produces a 97° rotational reorientation of the N-terminal domain relative to the C-terminal domain, clamping down on UDP and generating the binding site for 1-L-myo-inositol-1-phosphate. The structure highlights the residues important in binding of UDP-N-acetylglucosamine and 1-L-myo-inositol-1-phosphate. Molecular models of the ternary complex suggest a mechanism in which the β-phosphate of the substrate, UDP-N-acetylglucosamine, promotes the nucleophilic attack of the 3-hydroxyl group of 1-L-myo-inositol-1-phosphate while at the same time promoting the cleavage of the sugar nucleotide bond.

Received for publication, February 7, 2008 , and in revised form, March 26, 2008.

The atomic coordinates and structure factors (codes 3C48, 3C4Q, and 3C4V) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported, in whole or in part, by National Institutes of Health Grant AI33696 (to J. S. B.). This work was also supported by a fellowship from the Charles H. Revson Foundation (to P. A. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1–S7.

¹ To whom correspondence should be addressed: Dept. of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Tel.: 718-430-2785; Fax: 718-430-8565; E-mail: vetting{at}aecom.yu.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Yang, M. Ritchey, Y. Yoshida, C. A. Bush, and J. O. Cisar Comparative Structural and Molecular Characterization of Ribitol-5-Phosphate-Containing Streptococcus oralis Coaggregation Receptor Polysaccharides J. Bacteriol., March 15, 2009; 191(6): 1891 - 1900. [Abstract] [Full Text] [PDF]

				M. Barreras, S. R. Salinas, P. L. Abdian, M. A. Kampel, and L. Ielpi Structure and Mechanism of GumK, a Membrane-associated Glucuronosyltransferase J. Biol. Chem., September 5, 2008; 283(36): 25027 - 25035. [Abstract] [Full Text] [PDF]

				G. L. Newton, N. Buchmeier, and R. C. Fahey Biosynthesis and Functions of Mycothiol, the Unique Protective Thiol of Actinobacteria Microbiol. Mol. Biol. Rev., September 1, 2008; 72(3): 471 - 494. [Abstract] [Full Text] [PDF]