Crystallographic Structure and Thermostability of a Cu,Zn Superoxide Dismutase Mutant

A crystallographic structure of a bovine Cu,Zn superoxide dismutase mutant (Cys6→Ala) determined to 2.1-Å resolution. The dataset, from a study by Duncan E. McRee of Scripps Research Institute, characterizes the mutant's reversible and irreversible denaturation, including a delta delta G of 0.7-1.3 kcal/mol. It was used to analyze how small structural shifts reduce the energetic cost of an interior mutation in a Greek key beta-barrel fold.

Use Cases

• Analyzing the impact of single-point mutations on protein thermostability based on the described Cys6→Ala mutation.
• Studying the relationship between interior packing, hydrophobicity, and energetic cost in protein stability based on the described thermodynamic measurements.
• Modeling small concerted structural shifts in proteins based on the described atomic model refined to 2.1-Å resolution.
• Comparing reversible versus irreversible denaturation processes in protein design based on the experimental characterization described.

Strengths

• Atomic structure determined to a high resolution of 2.1 Å.
• Includes specific thermodynamic measurements, such as a delta delta G of 0.7-1.3 kcal/mol.
• Compares mutant and wild-type enzyme structures from isomorphous crystals.

Limitations

• Row count and specific column-level data are unknown, limiting suitability assessment.
• Description metadata is limited; actual data quality requires manual inspection after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

Scripps Research Institute

Collection Method

The recombinant protein was expressed in yeast, purified, characterized, crystallized, and its structure determined by X-ray diffraction and refinement with PROLSQ and X-PLOR.