Wheat Serine Carboxypeptidase II Structure at 3.5-A Resolution

A 3.5-angstrom resolution structure of serine carboxypeptidase II from wheat bran, determined by multiple isomorphous replacement and crystallographic refinement. The model was refined to a crystallographic R factor of 20.9% and reveals a catalytic triad similar to chymotrypsin but with a different protein fold. This work by D I Liao of the University of Oregon suggests a third example of convergent evolution in serine proteinases.

Use Cases

• Study convergent evolution in enzymes based on the described catalytic triad and novel protein fold.
• Validate or train protein structure prediction models based on the high-resolution crystallographic data.
• Analyze serine protease active site geometry based on the detailed structural model of Asp338, His397, and Ser146.
• Compare alpha+beta protein folds across different enzyme families as suggested by the similarity to carboxypeptidase A.

Strengths

• Structure determined to a specific 3.5-angstrom resolution.
• Model refined to a conventional crystallographic R factor of 20.9%.
• Includes a detailed description of the catalytic triad residues (Asp338, His397, Ser146).

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of Oregon

Collection Method

Multiple isomorphous replacement, solvent flattening, and crystallographic refinement.