The Interaction of a Carbohydrate-Binding Module from a Clostridium perfringens N-Acetyl-beta-hexosaminidase with its Carbohydrate Receptor

Journal Article · Sun Jan 01 00:00:00 EST 2006 · Journal of Biological Chemistry

DOI:https://doi.org/10.1074/jbc.M606126200· OSTI ID:959579

Ficko-Blean, E; Boraston, A

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-{beta}-hexosaminidase. Macroarray, UV difference, and isothermal titration calorimetry binding studies indicate a preference for the disaccharide LacNAc ({beta}-d-galactosyl-1,4-{beta}-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 Angstroms, respectively.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 959579
• Report Number(s): BNL-82565-2009-JA; JBCHA3; TRN: US201016%%723
• Journal Information: Journal of Biological Chemistry, Vol. 281, Issue 49; ISSN 0021-9258
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
AMINO ACID SEQUENCE
BLOOD GROUPS
CALORIMETRY
CARBOHYDRATES
CLOSTRIDIUM PERFRINGENS
DISACCHARIDES
ENZYMES
GALACTOSE
GASTROINTESTINAL TRACT
GLYCOSIDES
HYDROLASES
PATHOGENS
TITRATION
national synchrotron light source