2vno
From Proteopedia
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| - | [[Image:2vno.jpg|left|200px]] | + | [[Image:2vno.jpg|left|200px]] |
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| - | '''FAMILY 51 CARBOHYDRATE BINDING MODULE FROM A FAMILY 98 GLYCOSIDE HYDROLASE PRODUCED BY CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH BLOOD GROUP B-TRISACCHARIDE LIGAND.''' | + | {{Structure |
| + | |PDB= 2vno |SIZE=350|CAPTION= <scene name='initialview01'>2vno</scene>, resolution 1.45Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Binding+Site+For+Residue+Gal+B+1211'>AC1</scene>, <scene name='pdbsite=AC2:Binding+Site+For+Residue+Gal+B+1212'>AC2</scene>, <scene name='pdbsite=AC3:Binding+Site+For+Residue+Fuc+B+1213'>AC3</scene>, <scene name='pdbsite=AC4:Binding+Site+For+Residue+Gal+A+1210'>AC4</scene>, <scene name='pdbsite=AC5:Binding+Site+For+Residue+Gal+A+1211'>AC5</scene>, <scene name='pdbsite=AC6:Binding+Site+For+Residue+Fuc+A+1212'>AC6</scene>, <scene name='pdbsite=AC7:Binding+Site+For+Residue+Ca+A+1213'>AC7</scene> and <scene name='pdbsite=AC8:Binding+Site+For+Residue+Ca+B+1214'>AC8</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''FAMILY 51 CARBOHYDRATE BINDING MODULE FROM A FAMILY 98 GLYCOSIDE HYDROLASE PRODUCED BY CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH BLOOD GROUP B-TRISACCHARIDE LIGAND.''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2VNO is a [ | + | 2VNO 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=2VNO OCA]. |
==Reference== | ==Reference== | ||
| - | Divergent modes of glycan recognition by a new family of carbohydrate-binding modules., Gregg KJ, Finn R, Abbott DW, Boraston AB, J Biol Chem. 2008 Feb 21;. PMID:[http:// | + | Divergent modes of glycan recognition by a new family of carbohydrate-binding modules., Gregg KJ, Finn R, Abbott DW, Boraston AB, J Biol Chem. 2008 Feb 21;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18292090 18292090] |
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:47:50 2008'' |
Revision as of 16:47, 20 March 2008
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| , resolution 1.45Å | |||||||
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| Sites: | , , , , , , and | ||||||
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FAMILY 51 CARBOHYDRATE BINDING MODULE FROM A FAMILY 98 GLYCOSIDE HYDROLASE PRODUCED BY CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH BLOOD GROUP B-TRISACCHARIDE LIGAND.
Overview
The genomes of myonecrotic Clostridium perfringens isolates contain genes encoding a large and fascinating array of highly modular glycoside hydrolase enzymes. Though the catalytic activities of many of these enzymes are somewhat predictable based on their amino acid sequences the functions of their abundant ancillary modules are not and these remain poorly studied. Here we present the structural and functional analysis of a new family of ancillary carbohydrate-binding module (CBM), CBM51, which was previously annotated in databases as the NPCBM domain. The high resolution crystal structures of two CBM51 examples, GH95CBM51 and GH98CBM51, from a putative family 95 alpha-fucosidase and from a family 98 blood group A/B-antigen specific endo-beta-galactosidase, respectively, showed them to have highly similar beta-sandwich folds. However, GH95CBM51 was shown by glycan microarray screening, isothermal titration calorimetry, and X-ray crystallography to bind galactose residues while the same analysis of GH98CBM51 revealed specificity for the blood group A/B-antigens through non-conserved interactions. Overall, this work identifies a new family of CBMs with many members having apparent specificity for eukaryotic glycans, in keeping with the glycan rich environment C. perfringens would experience in its host. However, a wider bioinformatic analysis of this CBM family also indicated a large number of members in non-pathogenic environmental bacteria suggesting a role in the recognition of environmental glycans.
About this Structure
2VNO is a Single protein structure of sequence from Clostridium perfringens. Full crystallographic information is available from OCA.
Reference
Divergent modes of glycan recognition by a new family of carbohydrate-binding modules., Gregg KJ, Finn R, Abbott DW, Boraston AB, J Biol Chem. 2008 Feb 21;. PMID:18292090
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