2j1e: Difference between revisions
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|PDB= 2j1e |SIZE=350|CAPTION= <scene name='initialview01'>2j1e</scene>, resolution 2.40Å | |PDB= 2j1e |SIZE=350|CAPTION= <scene name='initialview01'>2j1e</scene>, resolution 2.40Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1e OCA], [http://www.ebi.ac.uk/pdbsum/2j1e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j1e RCSB]</span> | |||
}} | }} | ||
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[[Category: Boraston, A B.]] | [[Category: Boraston, A B.]] | ||
[[Category: Ficko-Blean, E.]] | [[Category: Ficko-Blean, E.]] | ||
[[Category: carbohydrate binding module]] | [[Category: carbohydrate binding module]] | ||
[[Category: cbm]] | [[Category: cbm]] | ||
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[[Category: protein-carbohydrate interaction]] | [[Category: protein-carbohydrate interaction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:51:46 2008'' | ||
Revision as of 03:51, 31 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HIGH RESOLUTION CRYSTAL STRUCTURE OF CBM32 FROM A N-ACETYL-BETA-HEXOSAMINIDASE IN COMPLEX WITH LACNAC
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
2J1E 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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