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PMID: 440298 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Staphylococcal nuclease reviewed: a prototypic study in contemporary enzymology. III. Correlation of the three-dimensional structure with the mechanisms of enzymatic action.

Molecular and cellular biochemistry ·Vol. 23 ·No. 2 ·1979-01-26 ·Pages 67-86

Tucker PW, Hazen EE, Cotton FA

Abstract

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.

MeSH Terms
Amino Acid Sequence Binding Sites Micrococcal Nuclease/metabolism Models, Molecular Peptide Fragments/analysis Protein Binding Protein Conformation Structure-Activity Relationship X-Ray Diffraction
Chemicals
Peptide Fragments Micrococcal Nuclease
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Tucker P W
Hazen E E
Cotton F A
References (53)
53 references, click to expand
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Article Info
Journal
Molecular and cellular biochemistry
Abbr.
Mol Cell Biochem
ISSN
0300-8177
DOI
10.1007/BF00226229
Published
1979-01-26
Pages
67-86
Language
English
Region
Netherlands
NLM ID
0364456
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00226229 View journal details
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