2c7f
From Proteopedia
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| - | [[Image:2c7f.gif|left|200px]]<br /><applet load="2c7f" size=" | + | [[Image:2c7f.gif|left|200px]]<br /><applet load="2c7f" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2c7f, resolution 2.70Å" /> | caption="2c7f, resolution 2.70Å" /> | ||
'''THE STRUCTURE OF A FAMILY 51 ARABINOFURANOSIDASE, ARAF51, FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH 1,5-ALPHA-L-ARABINOTRIOSE.'''<br /> | '''THE STRUCTURE OF A FAMILY 51 ARABINOFURANOSIDASE, ARAF51, FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH 1,5-ALPHA-L-ARABINOTRIOSE.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2C7F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-N-arabinofuranosidase Alpha-N-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] Known structural/functional Site: <scene name='pdbsite=AC1:Edo Binding Site For Chain F'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2C7F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-N-arabinofuranosidase Alpha-N-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] Known structural/functional Site: <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+F'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C7F OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylan]] | [[Category: xylan]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:32:23 2008'' |
Revision as of 08:32, 3 February 2008
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THE STRUCTURE OF A FAMILY 51 ARABINOFURANOSIDASE, ARAF51, FROM CLOSTRIDIUM THERMOCELLUM IN COMPLEX WITH 1,5-ALPHA-L-ARABINOTRIOSE.
Overview
The digestion of the plant cell wall requires the concerted action of a, diverse repertoire of enzyme activities. An important component of these, hydrolase consortia are arabinofuranosidases, which release, L-arabinofuranose moieties from a range of plant structural, polysaccharides. The anaerobic bacterium Clostridium thermocellum, a, highly efficient plant cell wall degrader, possesses a single, alpha-L-arabinofuranosidase (EC 3.2.1.55), CtAraf51A, located in GH51, (glycoside hydrolase family 51). The crystal structure of the enzyme has, been solved in native form and in 'Michaelis' complexes with both, alpha-1,5-linked arabinotriose and alpha-1,3 arabinoxylobiose, both, forming a hexamer in the asymmetric unit. Kinetic studies reveal that, CtAraf51A, in contrast with well-characterized GH51 enzymes including the, Cellvibrio japonicus enzyme [Beylot, McKie, Voragen, Doeswijk-Voragen and, Gilbert (2001) Biochem. J. 358, 607-614], catalyses the hydrolysis of, alpha-1,5-linked arabino-oligosaccharides and the alpha-1,3 arabinosyl, side chain decorations of xylan with equal efficiency. The paucity of, direct hydrogen bonds with the aglycone moiety and the flexible, conformation adopted by Trp(178), which stacks against the sugar at the +1, subsite, provide a structural explanation for the plasticity in substrate, specificity displayed by the clostridial arabinofuranosidase.
About this Structure
2C7F is a Single protein structure of sequence from Clostridium thermocellum with as ligand. Active as Alpha-N-arabinofuranosidase, with EC number 3.2.1.55 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum., Taylor EJ, Smith NL, Turkenburg JP, D'Souza S, Gilbert HJ, Davies GJ, Biochem J. 2006 Apr 1;395(1):31-7. PMID:16336192
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