Abstract
Catenulispora acidiphila is a newly identified lineage of actinomycetes that produces antimicrobial activities and represents a promising source of novel antibiotics and secondary metabolites. Among the discovered protein coding genes, 68 % were assigned a putative function, while the remaining 32 % are genes encoding "hypothetical" proteins. Caci-0382 is one of the "hypothetical" proteins that has very few homologs. Sequence analysis shows that the protein belongs to the NTF2-like protein family. The structure of Caci-0382 demonstrates that it shares the same fold and has a similar active site as limonene-1,2-epoxide hydrolase, which suggests that it may have a related function. Using a fluorescence thermal shift assay, we identified stabilizing compounds that suggest potential natural ligands of Caci-0382. Using this information, we determined the crystal structure in complex with trimethylamine to provide a better understanding of the function of this uncharacterized protein.
Original language | English (US) |
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Pages (from-to) | 33-40 |
Number of pages | 8 |
Journal | Journal of Structural and Functional Genomics |
Volume | 15 |
Issue number | 1 |
DOIs | |
State | Published - Mar 2014 |
Keywords
- Caci-0382
- NTF2-like superfamily
- Structural genomics
- Trimethylamine
- X-ray crystal structure
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics