2J1E

High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacNAc

Summary for 2J1E

• Entry DOI: 10.2210/pdb2j1e/pdb
• Related: 2CBI 2CBJ 2J1A 2J1F
• Related PRD ID: PRD_900019
• Descriptor: HYALURONIDASE, beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: protein-carbohydrate interactions, glycoside hydrolase, carbohydrate binding module, hydrolase, cbm
• Biological source: CLOSTRIDIUM PERFRINGENS
• Total number of polymer chains: 1
• Total formula weight: 16838.32

Authors

Ficko-Blean, E.,Boraston, A.B. (deposition date: 2006-08-10, release date: 2006-09-20, Last modification date: 2024-05-08)

Primary citation

Ficko-Blean, E.,Boraston, A.B.
The Interaction of a Carbohydrate-Binding Module from a Clostridium Perfringens N-Acetyl-Beta-Hexosaminidase with its Carbohydrate Receptor
J.Biol.Chem., 281:37748-, 2006

PubMed Abstract: 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 A, respectively.

PubMed: 16990278
DOI: 10.1074/JBC.M606126200

Experimental method

X-RAY DIFFRACTION (2.4 Å)