STAPHYLOCOCCAL NUCLEASE. PROPOSED MECHANISM OF ACTION BASED ON STRUCTURE OF ENZYME-THYMIDINE 3(PRIME),5(PRIME)-BIPHOSPHATE-CALCIUM ION COMPLEX AT 1.5-ANGSTROMS RESOLUTION
Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution.
STRUCTURE AND CONFORMATION OF NUCLEIC ACIDS AND PROTEIN-NUCLEIC ACID INTERACTIONS : PROCEEDINGS OF THE FOURTH ANNUAL HARRY STEENBOCK SYMPOSIUM, JUNE 16-19, 1974, MADISON, WISCONSIN
The Nucleotide Binding Site of Staphylococcal Nuclease and a New Approach to the Refinement of the Crystal Structures of Biological Macromolecules
Structure of Bis (Methylguanidinium) Monohydrogen Orthophosphate,A Model for the Arginine-Phosphate Interactions at the Active Site of Staphylococcal Nuclease and Other Phosphohydrolytic Enzymes
Some Aspects of the Structure of Staphylococcal Nuclease,Part I,Crystallographic Studies
Some Aspects of the Structure of Staphylococcal Nuclease,Part II,Studies in Solution
A High Resolution Structure of an Inhibitor Complex of the Extracellular Nuclease of Staphylococcus Aureus,I.Experimental Procedures and Chain Tracing
Thesis, Texas Agricultural and Mechanical University
National Biomedical Research Foundation, Silver Spring,Md.
Atlas of Protein Sequence and Structure (Data Section)
ATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMVENAKKIEVEFNKGQ RTDKYGRGLAYIYADGKMVNEALVRQGLAKVAYVYKPNNTHEQHLRKSEAQAKKEKLNIWSENDADSGQ
SHEET THERE ARE TWO BETA SHEETS WHICH FORM A DISTORTED VERSION OF A 5-STRANDED BETA BARREL. THE BARREL PATTERN IS -1,-1,+3, +1 IN THE NOTATION OF RICHARDSON.
THE ENZYME IS INACTIVE IN THE PRESENCE OF A CALCIUM ION AND THE MOLECULE THYMIDINE 3(PRIME)-5(PRIME) DIPHOSPHATE. THE STRUCTURE REPORTED HERE IS THE STRUCTURE WITH CALCIUM ION AND INHIBITOR BOUND.
THE ELECTRON DENSITY MAP DID NOT DISTINCTLY REVEAL THE LOCATION OF THE FIRST FIVE OR THE LAST EIGHT AMINO ACID RESIDUES (I.E. 1-5 AND 142-149). THE FIRST FIVE RESIDUES COULD BE FITTED TO THE WEAK DENSITY IN SEVERAL DIFFERENT CONFORMATIONS, BUT THERE WAS INSUFFICIENT DENSITY NEAR THE CARBOXY TERMINUS TO PERMIT ANY ATTEMPTS AT FITTING. ATOMIC COORDINATES FOR ALL FITTED ATOMS APPEAR IN THIS ENTRY.
STAPHYLOCOCCAL NUCLEASE (E.C.3.1.33.1) COMPLEX WITH 2(PRIME)-DEOXY-3(PRIME)-5(PRIME)-DIPHOSPHOTHYMIDINE
IDENTIFIES THE FOUR RESIDUES WHICH SUPPLY OXYGEN ATOMS TO BIND THE CALCIUM ION
RESIDUES WHICH BIND THE INHIBITOR MOLECULE