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Crystal structures of Streptomyces subtilisin inhibitor and its complex with subtilisin BPN′

Nature volume 277, pages 447–452 (1979)Cite this article

Abstract

Crystal structure of a microbial protein proteinase inhibitor SSI (Streptomyces subtilisin inhibitor) and its complex with subtilisin BPN′ were solved at 2.6 Å and 4.3 Å resolution respectively. The mode of binding to the proteinase of SSI is compared with that of bovine pancreatic trypsin inhibitor, soybean trypsin inhibitor and the substrates. Stereochemical considerations for the possible evolutionary relationship between SSI and pancreatic secretory trypsin inhibitor are presented.

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Author notes

  1. Y. Satow

    Present address: Laboratory of Molecular Biology, National Institute of Health, Bethesda, Maryland, 20014

Authors and Affiliations

  1. Faculty of Pharmaceutical Sciences, University of Tokyo, Hongo, Tokyo, 113, Japan

    Y. Mitsui, Y. Satow, Y. Watanabe, S. Hirono & Y. Iitaka

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  1. Y. Mitsui
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  2. Y. Satow
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  3. Y. Watanabe
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  4. S. Hirono
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  5. Y. Iitaka
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Mitsui, Y., Satow, Y., Watanabe, Y. et al. Crystal structures of Streptomyces subtilisin inhibitor and its complex with subtilisin BPN′. Nature 277, 447–452 (1979). https://doi.org/10.1038/277447a0

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