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A novel variant of the catalytic triad in the Streptomyces scabies esterase

Nature Structural Biology volume 2, pages 218–223 (1995)Cite this article

Abstract

The crystal structure of a novel esterase from Streptomyces scabies , a causal agent of the potato scab disease, was solved at 2.1 Å resolution. The tertiary fold of the enzyme is substantially different from that of the α/β hydrolase family and unique among all known hydrolases. The active site contains a dyad of Ser 14 and His 283, closely resembling two of the three components of typical Ser-His-Asp(Glu) triads from other serine hydrolases. Proper orientation of the active site imidazol is maintained by a hydrogen bond between the Nδ-H group and a main chain oxygen. Thus, the enzyme constitutes the first known natural variation of the chymotrypsin-like triad in which a carboxylic acid is replaced by a neutral hydrogen-bond acceptor.

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Authors and Affiliations

  1. Medical Research Council of Canada Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada

    Yunyi Wei, Urszula Derewenda, Lora Swenson & Zygmunt S. Derewenda

  2. Department of Biochemistry, University of Minnesota, St. Paul, Minnesota, USA

    Janet L. Schottel

  3. Novo-Nordisk Research Laboratories, Copenhagen, Denmark

    Shamkant Patkar

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  1. Yunyi Wei
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  2. Janet L. Schottel
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  3. Urszula Derewenda
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  4. Lora Swenson
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  5. Shamkant Patkar
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  6. Zygmunt S. Derewenda
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Wei, Y., Schottel, J., Derewenda, U. et al. A novel variant of the catalytic triad in the Streptomyces scabies esterase. Nat Struct Mol Biol 2, 218–223 (1995). https://doi.org/10.1038/nsb0395-218

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