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

AUTOR(ES)

Arnone, Arthur

RESUMO

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.

Documentos Relacionados

• Prediction of three-dimensional structures of enzyme-substrate and enzyme-inhibitor complexes of lysozyme.
• The reaction of fluorocitrate with aconitase and the crystal structure of the enzyme-inhibitor complex
• Enzyme-Inhibitor Association Thermodynamics: Explicit and Continuum Solvent Studies
• Surface-Bound Nuclease of Staphylococcus aureus: Localization of the Enzyme
• Latent tissue plasminogen activator produced by human endothelial cells in culture: evidence for an enzyme-inhibitor complex.