1cec | pdb_00001cec

A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES

spinqualitylabelsall models 1cec, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cec is a 1 chain structure with sequence from "ruminiclostridium_thermocellum"_yutin_and_galperin_2013 "ruminiclostridium thermocellum" yutin and galperin 2013. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: MC1061 ("Ruminiclostridium thermocellum" Yutin and Galperin 2013) Activity: Cellulase, with EC number 3.2.1.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GUNC_CLOTM] This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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