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J. Biol. Chem., Vol. 281, Issue 49, 37748-37757, December 8, 2006

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The Interaction of a Carbohydrate-binding Module from a Clostridium perfringens N-Acetyl--hexosaminidase with Its Carbohydrate Receptor^*

From the Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada

Clostridium perfringens is a notable colonizer of the human gastrointestinal tract. This bacterium is quite remarkable for a human pathogen by the number of glycoside hydrolases found in its genome. The modularity of these enzymes is striking as is the frequent occurrence of modules having amino acid sequence identity with family 32 carbohydrate-binding modules (CBMs), often referred to as F5/8 domains. Here we report the properties of family 32 CBMs from a C. perfringens N-acetyl--hexosaminidase. Macroarray, UV difference, and isothermal titration calorimetry binding studies indicate a preference for the disaccharide LacNAc (-D-galactosyl-1,4--D-N-acetylglucosamine). The molecular details of the interaction of this CBM with galactose, LacNAc, and the type II blood group H-trisaccharide are revealed by x-ray crystallographic studies at resolutions of 1.49, 2.4, and 2.3 Å, respectively.

Received for publication, June 27, 2006 , and in revised form, September 21, 2006.

The atomic coordinates and structure factors (code 2j1a, 2j1e, and 2j1f) 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 part by a grant from the Canadian Institutes for Health Research. 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 Fig. S1.

¹ Recipient of Doctoral Fellowships from the Michael Smith Foundation for Health Research and the National Science and Engineering Research Council of Canada.

² To whom correspondence should be addressed: Biochemistry & Microbiology, University of Victoria, P. O. Box 3055 STN CSC, Victoria, British Columbia V8W 3P6, Canada. Tel.: 250-472-4168; Fax: 250-721-8855; E-mail: boraston{at}uvic.ca.

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