1ga2: Difference between revisions

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~~'''~~THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE~~'''~~

===THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE===

~~==Overview==~~

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~~Complete cellulose degradation is the first step in the use of biomass as a source of renewable energy. To~~ this ~~end~~, ~~the engineering of novel cellulase activity~~, the ~~activity responsible for~~ the hydrolysis of the beta-1,4-glycosidic bonds in cellulose, is a topic of great interest. The high-resolution X-ray crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum has been determined at ~~a 1~~.~~6-A resolution~~. ~~The endoglucanase, Cel9G~~, is comprised of a family 9 catalytic domain attached to a family III(c) cellulose-binding domain. The two domains together form a flat platform onto which crystalline cellulose is suggested to bind and be fed into the ~~active-site cleft for endolytic hydrolysis~~. ~~To further dissect the structural basis of cellulose binding and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP~~-~~10 thio~~-~~oligosaccharide inhibitor were resolved at resolutions of 1.7, 1.8, and 1.9 A, respectively.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12837787}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12837787 is the PubMed ID number.

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==About this Structure==

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[[Category: Endoglucanase]]

[[Category: X-ray diffraction]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 17~~:20:08 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:58:29 2008''

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-[[Image:1ga2.jpg|left|200px]]
+{{Seed}}
+[[Image:1ga2.png|left|200px]]
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 {{STRUCTURE_1ga2|  PDB=1ga2  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE'''
+===THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM COMPLEXED WITH CELLOBIOSE===
-==Overview==
+<!--
-Complete cellulose degradation is the first step in the use of biomass as a source of renewable energy. To this end, the engineering of novel cellulase activity, the activity responsible for the hydrolysis of the beta-1,4-glycosidic bonds in cellulose, is a topic of great interest. The high-resolution X-ray crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum has been determined at a 1.6-A resolution. The endoglucanase, Cel9G, is comprised of a family 9 catalytic domain attached to a family III(c) cellulose-binding domain. The two domains together form a flat platform onto which crystalline cellulose is suggested to bind and be fed into the active-site cleft for endolytic hydrolysis. To further dissect the structural basis of cellulose binding and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were resolved at resolutions of 1.7, 1.8, and 1.9 A, respectively.
+The line below this paragraph, {{ABSTRACT_PUBMED_12837787}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12837787 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12837787}}
 ==About this Structure==
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 [[Category: Endoglucanase]]
 [[Category: X-ray diffraction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:20:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:58:29 2008''