2j7m: 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==

2J7M 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]]. This structure superseeds the now removed PDB entry 2J1F. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J7M OCA]].

2J7M 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]. This structure superseeds the now removed PDB entry 2J1F. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J7M OCA].

==Reference==

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[[Category: hydrolase]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on ~~Tue Oct 30 17~~:26:24 2007''

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:15:36 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==
-J7M 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]]. This structure superseeds the now removed PDB entry 2J1F. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J7M OCA]].
+J7M 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]. This structure superseeds the now removed PDB entry 2J1F. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J7M OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:26:24 2007''
+''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:15:36 2007''