1XYZ
A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES
Summary for 1XYZ
| Entry DOI | 10.2210/pdb1xyz/pdb |
| Descriptor | 1,4-BETA-D-XYLAN-XYLANOHYDROLASE (2 entities in total) |
| Functional Keywords | glycosyl hydrolase, xylanase, family f/10 of glycosyl hydrolases, clostridium thermocellum, glycosyltransferase |
| Biological source | Clostridium thermocellum |
| Total number of polymer chains | 2 |
| Total formula weight | 78868.45 |
| Authors | Alzari, P.M.,Spinelli, S.,Dominguez, R. (deposition date: 1995-06-07, release date: 1996-01-29, Last modification date: 2024-02-14) |
| Primary citation | Dominguez, R.,Souchon, H.,Spinelli, S.,Dauter, Z.,Wilson, K.S.,Chauvaux, S.,Beguin, P.,Alzari, P.M. A common protein fold and similar active site in two distinct families of beta-glycanases. Nat.Struct.Biol., 2:569-576, 1995 Cited by PubMed Abstract: 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. PubMed: 7664125DOI: 10.1038/nsb0795-569 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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