1k72
From Proteopedia
(New page: 200px<br /><applet load="1k72" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k72, resolution 1.80Å" /> '''The X-ray Crystal St...) |
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| - | [[Image:1k72.gif|left|200px]]<br /><applet load="1k72" size=" | + | [[Image:1k72.gif|left|200px]]<br /><applet load="1k72" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k72, resolution 1.80Å" /> | caption="1k72, resolution 1.80Å" /> | ||
'''The X-ray Crystal Structure Of Cel9G Complexed With cellotriose'''<br /> | '''The X-ray Crystal Structure Of Cel9G Complexed With cellotriose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Complete cellulose degradation is the first step in the use of biomass as | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1K72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum] with GLC, CBI, CA, MG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http:// | + | 1K72 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CBI:'>CBI</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K72 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Aghajari, N.]] | [[Category: Aghajari, N.]] | ||
[[Category: Belaich, A.]] | [[Category: Belaich, A.]] | ||
| - | [[Category: Belaich, J | + | [[Category: Belaich, J P.]] |
[[Category: Driguez, H.]] | [[Category: Driguez, H.]] | ||
[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:52 2008'' |
Revision as of 11:30, 21 February 2008
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The X-ray Crystal Structure Of Cel9G Complexed With cellotriose
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.
About this Structure
1K72 is a Single protein structure of sequence from Clostridium cellulolyticum with , , , and as ligands. Active as Cellulase, with EC number 3.2.1.4 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
Page seeded by OCA on Thu Feb 21 13:30:52 2008
Categories: Cellulase | Clostridium cellulolyticum | Single protein | Aghajari, N. | Belaich, A. | Belaich, J P. | Driguez, H. | Haser, R. | Mandelman, D. | CA | CBI | GLC | GOL | MG | (alpha-alpha)6-barrel | Cellotriose | Cellulose binding domain | Endoglucanase | Family 9 | X-ray diffraction
