1oc6
From Proteopedia
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| - | [[Image:1oc6.jpg|left|200px]]<br /><applet load="1oc6" size=" | + | [[Image:1oc6.jpg|left|200px]]<br /><applet load="1oc6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1oc6, resolution 1.50Å" /> | caption="1oc6, resolution 1.50Å" /> | ||
'''STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION'''<br /> | '''STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens] with NAG, CA and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Known structural/functional Site: <scene name='pdbsite=ACI:Gol Binding Site For Chain A'>ACI</scene>. Full crystallographic information is available from [http:// | + | 1OC6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Known structural/functional Site: <scene name='pdbsite=ACI:Gol+Binding+Site+For+Chain+A'>ACI</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OC6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: processive mechanism]] | [[Category: processive mechanism]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:56:04 2008'' |
Revision as of 07:56, 3 February 2008
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STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION
Overview
The enzymatic digestion of cellulose entails intimate involvement of, cellobiohydrolases, whose characteristic active-center tunnel contributes, to a processive degradation of the polysaccharide. The cellobiohydrolase, Cel6A displays an active site within a tunnel formed by two extended, loops, which are known to open and close in response to ligand binding., Here we present five structures of wild-type and mutant forms of Cel6A, from Humicola insolens in complex with nonhydrolyzable, thio-oligosaccharides, at resolutions from 1.7-1.1 A, dissecting the, structural accommodation of a processing substrate chain through the, active center during hydrolysis. Movement of ligand is facilitated by, extensive solvent-mediated interactions and through flexibility in the, hydrophobic surfaces provided by a sheath of tryptophan residues.
About this Structure
1OC6 is a Single protein structure of sequence from Humicola insolens with , and as ligands. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural basis for ligand binding and processivity in cellobiohydrolase Cel6A from Humicola insolens., Varrot A, Frandsen TP, von Ossowski I, Boyer V, Cottaz S, Driguez H, Schulein M, Davies GJ, Structure. 2003 Jul;11(7):855-64. PMID:12842048
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Categories: Cellulose 1,4-beta-cellobiosidase | Humicola insolens | Single protein | Boyer, V. | Davies, G.J. | Driguez, H. | Frandsen, T.P. | Ossowski, I.Von. | Schulein, M. | Varrot, A. | CA | GOL | NAG | Cellobiohydrolase | Cellulase | Cellulose degradation | Glycoside hydrolase family 6 | Hydrolase | Processive mechanism
