5YLO
Structural of Pseudomonas aeruginosa PA4980
Summary for 5YLO
| Entry DOI | 10.2210/pdb5ylo/pdb |
| Descriptor | Probable enoyl-CoA hydratase/isomerase, GLYCEROL (3 entities in total) |
| Functional Keywords | enoyl-coa hydratase activity, fatty acid beta-oxidation, hydrolase |
| Biological source | Pseudomonas aeruginosa PAO1 |
| Total number of polymer chains | 1 |
| Total formula weight | 29045.86 |
| Authors | Liu, L.,Li, T.,Peng, C.T.,Li, C.C.,Xiao, Q.J.,He, L.H.,Wang, N.Y.,Bao, R. (deposition date: 2017-10-18, release date: 2018-08-22, Last modification date: 2024-03-27) |
| Primary citation | Liu, L.,Li, T.,Peng, C.T.,Sun, C.Z.,Li, C.C.,Xiao, Q.J.,He, L.H.,Wang, N.Y.,Song, Y.J.,Zhu, Y.B.,Li, H.,Kang, M.,Tang, H.,Xiong, X.,Bao, R. Structural characterization of a Delta3, Delta2-enoyl-CoA isomerase from Pseudomonas aeruginosa: implications for its involvement in unsaturated fatty acid metabolism. J.Biomol.Struct.Dyn., 37:2695-2702, 2019 Cited by PubMed 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. PubMed: 30052139DOI: 10.1080/07391102.2018.1495102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.39 Å) |
Structure validation
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