A 2.1-Å resolution crystal structure of PbAcE, a cold-active acetyl xylan esterase isolated from Paenibacillus sp. R4, was solved to investigate its active site and low-temperature activity. Structural analysis revealed a hexameric enzyme with a central substrate binding tunnel, weak inter-subunit interactions, and specific loop conformations. The dataset, contributed by AMD_KOPRI and hosted on NASA Earthdata, was last updated in July 2018.
Use Cases
- Analyzing enzyme structure for low-temperature activity based on the solved crystal structure
- Investigating substrate binding site conformation based on the described β4–α3 and β5–α4 loop regions
- Comparing inter-subunit interactions for thermal adaptation based on the comparison with mesophilic and thermophilic homologs
- Evaluating enzyme activity against antibiotic substrates based on the mention of cefotaxime and 7-ACA
- Providing a template for structure-based protein engineering based on the conclusion of the manuscript
Strengths
- The crystal structure was solved at a high resolution of 2.1 Å
- The enzyme's activity was characterized at specific temperatures (4°C and 25°C)
- The manuscript provides a detailed structural analysis of the hexameric enzyme and its active site
Limitations
- Column-level documentation is absent; field semantics must be inferred after download
- Last updated 2018-07-26 23:59:59.999000; freshness should be verified
- Row count is unknown, which may limit suitability assessment
Provenance
- Source
- AMD_KOPRI
- Collection Method
- Likely involves X-ray crystallography and biochemical characterization as described in the manuscript.