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1g87

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{{STRUCTURE_1g87| PDB=1g87 | SCENE= }}
{{STRUCTURE_1g87| PDB=1g87 | SCENE= }}
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'''THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM'''
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===THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM===
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==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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12837787 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12837787}}
==About this Structure==
==About this Structure==
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[[Category: Endoglucanase]]
[[Category: Endoglucanase]]
[[Category: X-ray diffraction]]
[[Category: X-ray diffraction]]
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Revision as of 01:52, 1 July 2008

Image:1g87.png

Template:STRUCTURE 1g87

THE CRYSTAL STRUCTURE OF ENDOGLUCANASE 9G FROM CLOSTRIDIUM CELLULOLYTICUM

Template:ABSTRACT PUBMED 12837787

About this Structure

1G87 is a Single protein structure of sequence from Clostridium cellulolyticum. Full crystallographic information is available from OCA.

Reference

X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides., Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R, J Bacteriol. 2003 Jul;185(14):4127-35. PMID:12837787

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