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A common protein fold and similar active site in two distinct families of β-glycanases

Nature Structural Biology volume 2, pages 569–576 (1995)Cite this article

Abstract

The structure of Clostridium thermocellum endoglucanase CeIC, a member of the largest cellulase family (family A), has been determined at 2.15 Å resolution. The protein folds into an (α/β)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 Å 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 CeIC are similar, suggesting a common evolutionary origin.

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Author notes

  1. Silvia Spinelli

    Present address: LCCMB, Faculté de Médecine, Secteur Nord, 13916, Marseille, Cedex 20, France

Authors and Affiliations

  1. Unité d'lmmunologie Structural, URA 1961 CNRS, Institut Pasteur, 75724, Paris, Cedex 15, France

    Roberto Dominguez, Hélène Souchon, Silvia Spinelli & Pedro M. Alzari

  2. Unité de Physiologie Cellulaire, URA 1300 CNRS, Institut Pasteur, 75724, Paris, Cedex 15, France

    Sylvie Chauvaux & Pierre Béguin

  3. EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-2000, Hamburg, 52, Germany

    Zbigniew Dauter & Keith S. Wilson

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  1. Roberto Dominguez
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  2. Hélène Souchon
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  7. Pierre Béguin
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Dominguez, R., Souchon, H., Spinelli, S. et al. A common protein fold and similar active site in two distinct families of β-glycanases. Nat Struct Mol Biol 2, 569–576 (1995). https://doi.org/10.1038/nsb0795-569

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