2j1a: Difference between revisions

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==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 ... ~~[[http://ispc~~.~~weizmann.ac.il/pmbin/getpm?16990278 (full description)]]~~

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==

2J1A 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 GAL and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J1A OCA]].

2J1A 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 GAL and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J1A OCA].

==Reference==

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[[Category: protein-carbohydrate interaction]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on ~~Tue Oct 30 17~~:21:43 2007''

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:14:33 2007''

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@@ Line 5: / Line 5: @@
 ==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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16990278 (full description)]]
+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==
-J1A 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 GAL and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J1A OCA]].
+J1A 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 GAL and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J1A OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: protein-carbohydrate interaction]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:21:43 2007''
+''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 13:14:33 2007''