By the same authors

From the same journal

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

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Author(s)

  • R DOMINGUEZ
  • H SOUCHON
  • S SPINELLI
  • Z DAUTER
  • K S WILSON
  • S CHAUVAUX
  • P BEGUIN
  • P M ALZARI

Department/unit(s)

Publication details

JournalNature Structural Biology
DatePublished - Jul 1995
Issue number7
Volume2
Number of pages8
Pages (from-to)569-576
Original languageEnglish

Abstract

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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