Article
Active site mutant Glu-43----Asp in staphylococcal nuclease displays nonlocal structural changes.
Biochemistry - 24 Jul 1990
Loll P J, Lattman E E
Abstract excerpt
The crystal structure of the Glu-43----Asp mutant of staphylococcal nuclease complexed with Ca2+ and the inhibitor thymidine 3',5'-bisphosphate (pdTp) has been determined and refined by restrained least-squares methods to a conventional crystallographic R value of 0.174 at a resolution of 1.74 A. Throughout most of the structure, the conformation of the backbone atoms of the mutant is similar to that of the...
Topics
- Binding Sites
- Crystallography
- Magnetic Resonance Spectroscopy
- Micrococcal Nuclease
- Models, Molecular
- Molecular Structure
- Mutation
- Protein Conformation
