2j1a: Difference between revisions

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[[Image:2j1a.gif|left|200px]]<br /><applet load="2j1a" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2j1a.gif|left|200px]]
caption="2j1a, resolution 1.49&Aring;" />
 
'''STRUCTURE OF CBM32 FROM CLOSTRIDIUM PERFRINGENS BETA-N-ACETYLHEXOSAMINIDASE GH84C IN COMPLEX WITH GALACTOSE'''<br />
{{Structure
|PDB= 2j1a |SIZE=350|CAPTION= <scene name='initialview01'>2j1a</scene>, resolution 1.49&Aring;
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY=
|GENE=
}}
 
'''STRUCTURE OF CBM32 FROM CLOSTRIDIUM PERFRINGENS BETA-N-ACETYLHEXOSAMINIDASE GH84C IN COMPLEX WITH GALACTOSE'''
 


==Overview==
==Overview==
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==About this Structure==
==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 <scene name='pdbligand=GAL:'>GAL</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J1A OCA].  
2J1A is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J1A OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16990278 16990278]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16990278 16990278]
[[Category: Clostridium perfringens]]
[[Category: Clostridium perfringens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: protein-carbohydrate interaction]]
[[Category: protein-carbohydrate interaction]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:58:16 2008''
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Revision as of 18:36, 20 March 2008

File:2j1a.gif


PDB ID 2j1a

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, resolution 1.49Å
Sites:
Ligands: and
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF CBM32 FROM CLOSTRIDIUM PERFRINGENS BETA-N-ACETYLHEXOSAMINIDASE GH84C IN COMPLEX WITH GALACTOSE


OverviewOverview

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 StructureAbout this Structure

2J1A is a Single protein structure of sequence from Clostridium perfringens. Full crystallographic information is available from OCA.

ReferenceReference

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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