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

J Biomol Struct Dyn. 2019 Jul;37(10):2695-2702. doi: 10.1080/07391102.2018.1495102. Epub 2018 Nov 17.

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: crystal structure; diffusible signal factors; isomerase; unsaturated fatty acid.

MeSH terms

  • Amino Acid Sequence
  • Dodecenoyl-CoA Isomerase / chemistry*
  • Dodecenoyl-CoA Isomerase / metabolism
  • Fatty Acids, Unsaturated / chemistry
  • Fatty Acids, Unsaturated / metabolism
  • Isomerases / chemistry
  • Isomerases / metabolism
  • Lipid Metabolism
  • Models, Molecular*
  • Molecular Dynamics Simulation
  • Protein Array Analysis
  • Protein Binding
  • Protein Conformation*
  • Pseudomonas aeruginosa / enzymology*
  • Structure-Activity Relationship

Substances

  • Fatty Acids, Unsaturated
  • Isomerases
  • Dodecenoyl-CoA Isomerase