1cec
From Proteopedia
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A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES
Overview
The structure of Clostridium thermocellum endoglucanase CelC, a member of the largest cellulase family (family A), has been determined at 2.15 A resolution. The protein folds into an (alpha/beta)8 barrel, with a deep active-site cleft generated by the insertion of a helical subdomain. The structure of the catalytic core of xylanase XynZ, which belongs to xylanase family F, has been determined at 1.4 A resolution. In spite of significant differences in substrate specificity and structure (including the absence of the helical subdomain), the general polypeptide folding pattern, architecture of the active site and catalytic mechanism of XynZ and CelC are similar, suggesting a common evolutionary origin.
About this Structure
1CEC is a Single protein structure of sequence from Clostridium thermocellum. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.
Reference
A common protein fold and similar active site in two distinct families of beta-glycanases., Dominguez R, Souchon H, Spinelli S, Dauter Z, Wilson KS, Chauvaux S, Beguin P, Alzari PM, Nat Struct Biol. 1995 Jul;2(7):569-76. PMID:7664125
Page seeded by OCA on Thu Feb 21 12:05:11 2008
