2vno: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:2vno.jpg|left|200px]]
{{Seed}}
[[Image:2vno.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vno|  PDB=2vno  |  SCENE=  }}  
{{STRUCTURE_2vno|  PDB=2vno  |  SCENE=  }}  


'''FAMILY 51 CARBOHYDRATE BINDING MODULE FROM A FAMILY 98 GLYCOSIDE HYDROLASE PRODUCED BY CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH BLOOD GROUP B-TRISACCHARIDE LIGAND.'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_18292090}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18292090 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18292090}}


==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Family 98 glycoside hydrolase]]
[[Category: Family 98 glycoside hydrolase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 19:02:55 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:10:26 2008''

Revision as of 00:10, 29 July 2008

File:2vno.png

Template:STRUCTURE 2vno

FAMILY 51 CARBOHYDRATE BINDING MODULE FROM A FAMILY 98 GLYCOSIDE HYDROLASE PRODUCED BY CLOSTRIDIUM PERFRINGENS IN COMPLEX WITH BLOOD GROUP B-TRISACCHARIDE LIGAND.

Template:ABSTRACT PUBMED 18292090

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

Page seeded by OCA on Tue Jul 29 03:10:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2vno&oldid=724473"