Crystal Structures of a Psychrophilic Bacterial Isoaspartyl Dipeptidase

Crystal structure and functional characterization of an isoaspartyl dipeptidase (CpsIadA) from Colwellia psychrerythraea strain 34H. The dataset includes structures for both ligand-free and ligand-complexed forms at 1.85-Å and 2.33-Å resolution, respectively. It was produced by AMD_KOPRI and published in 2017.

Use Cases

• Compare active site residue composition (Glu166 vs. carbamylated-lysine) between Type I and Type II IadA enzymes.
• Analyze the structural impact of the β12-α8 loop protrusion on substrate-binding pocket conformation.
• Model enzyme-substrate interactions using the β-isoaspartyl lysine complex structure.
• Investigate the relationship between octameric quaternary structure and thermostability in psychrophilic enzymes.
• Determine substrate specificity profiles based on active-site structural comparisons with Escherichia coli IadA.

Strengths

• High-resolution crystal structures at 1.85-Å and 2.33-Å resolution.
• Includes both ligand-free and ligand-complexed structural forms for comparative analysis.
• Provides conclusive first description of a Type I IadA enzyme structure.

Limitations

• Sample size is limited to a single enzyme from one bacterial strain.
• No kinetic or thermodynamic data beyond pH and temperature optima is provided in the description.
• The dataset is from 2017 and may not reflect the most recent research.

Provenance

Source

AMD_KOPRI via NASA Earthdata.

Collection Method

X-ray crystallography and site-directed mutagenesis studies.

Freshness

2017-06-21

Geography

Enzyme isolated from Colwellia psychrerythraea strain 34H, a psychrophilic bacterium.