| Autor: |
Filippova EV; Department of Molecular Pharmacology and Biological Chemistry, Northwestern Feinberg School of Medicine, Chicago, IL, 60611, USA., Luan CH, Dunne SF, Kiryukhina O, Minasov G, Shuvalova L, Anderson WF |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of structural and functional genomics [J Struct Funct Genomics] 2014 Mar; Vol. 15 (1), pp. 33-40. Date of Electronic Publication: 2014 Feb 22. |
| DOI: |
10.1007/s10969-014-9176-z |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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