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. 1969 Oct;64(2):420–427. doi: 10.1073/pnas.64.2.420

THE EXTRACELLULAR NUCLEASE OF Staphylococcus aureus: STRUCTURES OF THE NATIVE ENZYME AND AN ENZYME-INHIBITOR COMPLEX AT 4 Å RESOLUTION*

Arthur Arnone 1,†, C James Bier 1, F Albert Cotton 1, Edward E Hazen Jr 1, David C Richardson 1, Jane S Richardson 1
PMCID: PMC223359  PMID: 5261023

Abstract

Independent 4 Å electron density maps calculated for the extracellular nuclease of Staphylococcus aureus (based on data from three heavy-atom derivatives) and for a nuclease-thymidine-3′,5′-diphosphate-calcium ion complex (based on a single isomorphous derivative) show about 60 per cent of the chain resolved, including 3½ turns of helix. The pyrimidine ring of the inhibitor fits into a pocket in the enzyme and appears to be parallel to the ring of a tyrosyl residue. Conformational changes can be observed between the nuclease and the nuclease-inhibitor complex, but the two structures seem to be identical over most of the molecule.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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