1oa7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1oa7.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1oa7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1oa7| PDB=1oa7 | SCENE= }}
{{STRUCTURE_1oa7| PDB=1oa7 | SCENE= }}
-
'''STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE'''
+
===STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE===
-
==Overview==
+
<!--
-
Cellulose, a polysaccharide of beta-1,4-linked D-glucosyl units, is the major component of plant cell walls and one of the most abundant biopolymers in nature. Cellulases (cellobiohydrolases and endoglucanases) are enzymes that catalyse the hydrolysis of cellulose to smaller oligosaccharides, a process of paramount importance in biotechnology. The thermophilic fungus Melanocarpus albomyces produces a 20 kDa endoglucanase known as 20K-cellulase that has been found particularly useful in the textile industry. The crystal structures of free 20K-cellulase and its complex with cellobiose have been determined at 2.0 A resolution. The enzyme, classified into the glycoside hydrolase family 45, exhibits the characteristic six-stranded beta-barrel found before in Humicola insolens endoglucanase V structure. However, the active site in the 20K-cellulase shows a closing of approximately 2.5-3.5A while a mobile loop identified previously in Humicola insolens endoglucanase V and implicated in the catalytic mechanism is well-defined in 20K-cellulase. In addition, the crystal structure of the cellobiose complex shows a shift in the cellobiose position at the substrate-binding cleft. It is therefore proposed that these alterations may reflect differences in the binding mechanism and catalytic action of the enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12767825}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12767825 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12767825}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Cellulose degradation]]
[[Category: Cellulose degradation]]
[[Category: Glycoside hydrolase]]
[[Category: Glycoside hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:35:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:05:13 2008''

Revision as of 20:05, 27 July 2008

Image:1oa7.png

Template:STRUCTURE 1oa7

STRUCTURE OF MELANOCARPUS ALBOMYCES ENDOGLUCANASE IN COMPLEX WITH CELLOBIOSE

Template:ABSTRACT PUBMED 12767825

About this Structure

1OA7 is a Single protein structure of sequence from Melanocarpus albomyces. Full crystallographic information is available from OCA.

Reference

Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: mechanistic implications based on the free and cellobiose-bound forms., Hirvonen M, Papageorgiou AC, J Mol Biol. 2003 Jun 6;329(3):403-10. PMID:12767825

Page seeded by OCA on Sun Jul 27 23:05:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1oa7"
Personal tools