Aquifex Aeolicus Dihydroorotase Structure Under High Hydrostatic Pressure

Dihydroorotase from the hyperthermophilic bacterium Aquifex aeolicus was studied under 600 bar of hydrostatic pressure. The crystallographic structure determination demonstrates pressure-induced reactivation involves loop displacement and catalytic site rearrangement. The dataset was produced by T. Prangé of the Centre National de la Recherche Scientifique.

Use Cases

• Modeling enzyme reactivation mechanisms based on pressure-induced structural changes described in the study
• Analyzing protein-ligand interactions in the catalytic site based on the rearrangement of aspartate 305
• Studying the relationship between ionic interactions, loop mobility, and enzyme activity as inferred from the kinetic and mutagenesis data
• Comparing the structure of isolated DHOase with its noncovalently associated form with aspartate transcarbamylase

Strengths

• Focuses on a specific enzyme, dihydroorotase, from a hyperthermophilic organism
• Investigates a precise experimental condition of 600 bar hydrostatic pressure
• Integrates crystallographic structure data with kinetic studies and site-directed mutagenesis

Limitations

• Row count is unknown, which may limit suitability assessment
• Column-level documentation is absent; field semantics must be inferred after download
• Data may reflect the specific experimental bias inherent to paperswithcode

Provenance

Source

Centre National de la Recherche Scientifique

Collection Method

Crystallographic structure determination under pressure, complemented by kinetic studies and site-directed mutagenesis.