2J1A
Structure of CBM32 from Clostridium perfringens beta-N- acetylhexosaminidase GH84C in complex with galactose
Summary for 2J1A
| Entry DOI | 10.2210/pdb2j1a/pdb |
| Related | 2CBI 2CBJ 2J1E 2J1F |
| Descriptor | HYALURONIDASE, beta-D-galactopyranose, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | protein-carbohydrate interaction, glycoside hydrolase, cbm32, gh84c, hydrolase |
| Biological source | CLOSTRIDIUM PERFRINGENS |
| Total number of polymer chains | 1 |
| Total formula weight | 16635.12 |
| Authors | Ficko-Blean, E.,Boraston, A.B. (deposition date: 2006-08-09, release date: 2006-08-22, 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 Cited by 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: 16990278DOI: 10.1074/JBC.M606126200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.49 Å) |
Structure validation
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