Structural characterization of a Δ³, Δ²-enoyl-CoA isomerase from Pseudomonas aeruginosa: implications for its involvement in unsaturated fatty acid metabolism

Abstract

Gene PA4980 from Pseudomonas aeruginosa encodes a putative enoyl-coenzyme A hydratase/isomerase that is associated with the function of the biofilm dispersion-inducing signal molecule cis-2-decenoic acid. To elucidate the role of PA4980 in cis-2-decenoic acid biosynthesis, we reported the crystal structure of its protein product at 2.39 Å. The structural analysis and substrate binding prediction suggest that it acts as a monofunctional enoyl-coenzyme A isomerase, implicating an alternative pathway of the cis-2-decenoic acid synthesis.

Keywords:

• Pseudomonas aeruginosa
• diffusible signal factors
• unsaturated fatty acid
• isomerase
• crystal structure

Acknowledegment

We thank SSRF beamline BL17U for beamtime allowance. We thank the staffs of National Center for Protein Sciences Shanghai (NCPSS) beamlines BL18U and BL19U and SSRF, Shanghai, People’s Republic of China, for assistance during data collection.

Disclosure statement

No potential conflict of interest was reported by the author(s).

Accession codes

Atomic coordinates of the refined structures have been deposited in the Protein Data Bank (www.pdb.org) with the PDB code 5YLO.

Additional information

Funding

The work was supported by National Key Research and Development Plan (Grant No. SQ2016YFJC040104), National Natural Science Foundation of China (Grant No. 81670008 and 81501787) and PhD Research Foundation of the Affiliated Hospital of Southwest Medical University.