2c7f
From Proteopedia
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. 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 Page seeded by OCA on Sat May 3 21:22:45 2008
