Research output: Contribution to journal › Article › peer-review
Journal | Nature Structural Biology |
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Date | Published - Jul 1995 |
Issue number | 7 |
Volume | 2 |
Number of pages | 8 |
Pages (from-to) | 569-576 |
Original language | English |
The structure of Clostridium thermocellum endoglucanase CelC, a member of the largest cellulase family (family A), has been determined at 2.15 Angstrom 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 Angstrom 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 ave similar, suggesting a common evolutionary origin.
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