Some Aspects of the Structure of Staphylococcal Nuclease: PART I. CRYSTALLOGRAPHIC STUDIES

Abstract

We will make no attempt here to present a complete description of either the crystal structure of the complex between the staphylococcal nuclease, thymidine-3′,5′-diphosphate (pdTp) and calcium ion or of the behavior of the enzyme in solution. Rather we restrict ourselves, in the first part, to (a) preliminary consideration of some of the interactions of the amino acid side chains, and (b) a brief and speculative proposal concerning the mechanism of action for the nuclease. In the second section, we shall summarize certain solution studies of this enzyme, namely those concerning the course of denaturation-renaturation and the recombination of the various fragmented forms of the nuclease and attempt to correlate these with the structure. The chemistry and structure of the nuclease are reviewed in some detail in two chapters in The Enzymes (Anfinsen et al., 1971; Cotton and Hazen, 1971).