Crystal structures of two forms of the UbiX enzyme from the psychrophilic bacterium Colwellia psychrerythraea, including an FMN-bound wild type and an FMN-unbound mutant. The dataset provides atomic-level structural data revealing novel FMN-binding domain architecture and FMN-induced conformational changes in the C-terminal loop. The structural data was produced by the AMD_KOPRI organization and published in 2015.
Use Cases
- Analyze the novel FMN-binding domain architecture formed by three neighboring subunits to understand unique protein assembly.
- Compare the FMN-bound wild type and FMN-unbound V47S mutant structures to model conformational changes in the C-terminal loop region (residues 170–177 and 195–206).
- Study the roles of conserved residues Gly15, Ser41, Val47, and Tyr171 in FMN binding through structural analysis.
- Use the structural framework to model substrate binding mechanisms, informed by the described liposome binding assay results.
- Investigate the dodecameric Rossmann-fold structure of CpsUbiX for comparative studies with other decarboxylases.
Strengths
- Provides atomic-resolution 3D structures for two distinct protein states (FMN-bound and unbound).
- Identifies a novel FMN-binding domain architecture unique to the UbiX enzyme family.
- Structural analysis is supported by computational modeling and a liposome binding assay.
Limitations
- Dataset size and specific row/column counts are unknown.
- Data is from a single study on one bacterial strain, limiting generalizability.
- The data is from 2015 and may not reflect the most recent research.
Provenance
- Source
- AMD_KOPRI organization, via NASA Earthdata.
- Collection Method
- X-ray crystallography experiments on purified CpsUbiX protein.
- Time Range
- null
- Freshness
- Last updated 2015-10-06.
- Geography
- null