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

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 inhibito...

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Bibliographic Details
Published in:Nature (London) 1979-02, Vol.277 (5696), p.447-452
Main Authors: Mitsui, Y, Satow, Y, Watanabe, Y, Hirono, S, Iitaka, Y
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Biological Evolution
Crystallography
Humanities and Social Sciences
multidisciplinary
Protease Inhibitors - metabolism
Protein Binding
Protein Conformation
Science
Science (multidisciplinary)
Streptomyces - enzymology
Substrate Specificity
Subtilisins - antagonists & inhibitors
Subtilisins - metabolism
Trypsin Inhibitor, Kazal Pancreatic - genetics
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/277447a0