2j1e
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 ... | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2J1E is a | + | 2J1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J1E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein-carbohydrate interactions]] | [[Category: protein-carbohydrate interactions]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:14:44 2007'' |
Revision as of 11:09, 5 November 2007
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HIGH RESOLUTION CRYSTAL STRUCTURE OF CBM32 FROM A N-ACETYL-BETA-HEXOSAMINIDASE IN COMPLEX WITH LACNAC
Overview
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.
About this Structure
2J1E is a Single protein structure of sequence from Clostridium perfringens with CA as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor., Ficko-Blean E, Boraston AB, J Biol Chem. 2006 Dec 8;281(49):37748-57. Epub 2006 Sep 21. PMID:16990278
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