Download MendeleyCrystal structure of oleate hydratase from Stenotrophomonas sp. KCTC 12332 reveals conformational plasticity surrounding the FAD binding site.
Park, A.K., Lee, G.H., Kim, D.W., Jang, E.H., Kwon, H.T., Chi, Y.M.(2018) Biochem Biophys Res Commun 499: 772-776
- PubMed: 29608896
- DOI: https://doi.org/10.1016/j.bbrc.2018.03.220
- Primary Citation of Related Structures:
5Z70 - PubMed Abstract:
Unsaturated fatty acids are toxic to various bacteria, causing their death or growth inhibition. To prevent this toxicity, unsaturated fatty acids should be converted into saturated fatty acids via hydrogenation reaction, which is the complete reduction of double bonds on the carbon chain. In a recent report, we observed that Stenotrophomonas sp. KCTC 12332 exhibited a high biotransformation activity of oleic acid (OA) in 10-hydroxystearic acid and identified the gene encoding oleate hydratase (OhySt) by complete genomic analysis. In the present study, to further investigate the structural features of OhySt, the recombinant protein was expressed in Escherichia coli, and then purified and crystallized. Biochemical assay showed that OhySt produces 10-hydroxystearic acid in a flavin adenosine dinucleotide (FAD)-dependent manner, indicating that it requires FAD as a cofactor. The OhySt structure, which is determined in its apo state, allows for a structural comparison with the previously reported FAD bound structure of oleate hydratase. The comparison of structures indicates remarkable conformational change of the loop region surrounding the FAD molecule upon binding of FAD. This change forces one of the important catalytic residues into position for catalysis.
Organizational Affiliation:
Division of Biotechnology, College of Life Sciences, Korea University, Seoul, 02841, Republic of Korea; Unit of Polar Genomics, Korea Polar Research Institute, Yeonsu-gu, Incheon, 21990, Republic of Korea.
