2pc8
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
- | [[Image:2pc8.png|left|200px]] | ||
- | |||
{{STRUCTURE_2pc8| PDB=2pc8 | SCENE= }} | {{STRUCTURE_2pc8| PDB=2pc8 | SCENE= }} | ||
- | |||
===E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two separately bound glucopyranoside units at 1.8 A=== | ===E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two separately bound glucopyranoside units at 1.8 A=== | ||
+ | {{ABSTRACT_PUBMED_20875088}} | ||
- | + | ==Function== | |
+ | [[http://www.uniprot.org/uniprot/EXG_CANAL EXG_CANAL]] Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase. | ||
==About this Structure== | ==About this Structure== | ||
Line 11: | Line 10: | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:020875088</ref>< | + | <ref group="xtra">PMID:020875088</ref><references group="xtra"/><references/> |
[[Category: Candida albicans]] | [[Category: Candida albicans]] | ||
[[Category: Glucan 1,3-beta-glucosidase]] | [[Category: Glucan 1,3-beta-glucosidase]] |
Revision as of 08:54, 19 June 2013
Contents |
E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two separately bound glucopyranoside units at 1.8 A
Template:ABSTRACT PUBMED 20875088
Function
[EXG_CANAL] Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase.
About this Structure
2pc8 is a 1 chain structure with sequence from Candida albicans. Full crystallographic information is available from OCA.
Reference
- Patrick WM, Nakatani Y, Cutfield SM, Sharpe ML, Ramsay RJ, Cutfield JF. Carbohydrate binding sites in Candida albicans exo-beta-1,3-glucanase and the role of the Phe-Phe 'clamp' at the active site entrance. FEBS J. 2010 Sep 10. doi: 10.1111/j.1742-4658.2010.07869.x. PMID:20875088 doi:10.1111/j.1742-4658.2010.07869.x