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Staphylococcal nuclease reviewed: A prototypic study in contemporary enzymology

III. Correlation of the three-dimensional structure with the mechanisms of enzymatic action

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Summary

This is the third in a series of four articles in which the chemical, enzymological and crystallographic work on Ribonucleate (deoxribonucleate)-3′-nucleotidohydrolase, EC 3.1.4.4 (staphylococcal nuclease, micrococcal nuclease) will be reviewed and correlated. This article describes the structure of the nuclease and of a nuclease-inhibitor complex as determined by x-ray crystallography. The crystal structures are correlated with some of the known chemical and enzymological properties of the enzyme, and the three areas combined to propose a mechanism of action.

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Authors and Affiliations

  1. Laboratory of Genetics, University of Wisconsin-Madison, 53706, Madison, Wisconsin

    Philip W. Tucker

  2. Department of Chemistry, Texas A & M University, 77843, College Station, Texas

    F. Albert Cotton

Authors
  1. Philip W. Tucker
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  2. Edward E. Hazen Jr.
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  3. F. Albert Cotton
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Additional information

This article is the third in a series of four devoted to the stapholoccal nuclease. Reviews concerning its isolation and enzymology (1) as well as the features of its ligand binding site (2) have appeared in previous issues. Work from this laboratory has been supported by grants from the National Institute of General Medical Sciences, NIH and from the Robert A. Welch Foundation to F. A. Cotton and E. E. Hazen, Jr.

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Tucker, P.W., Hazen, E.E. & Cotton, F.A. Staphylococcal nuclease reviewed: A prototypic study in contemporary enzymology. Mol Cell Biochem 23, 67–86 (1979). https://doi.org/10.1007/BF00226229

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  • DOI: https://doi.org/10.1007/BF00226229

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