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Structural characterization of a Δ3, Δ2-enoyl-CoA isomerase from Pseudomonas aeruginosa: implications for its involvement in unsaturated fatty acid metabolism
Version 2 2018-11-17, 17:04Version 2 2018-11-17, 17:04
Version 1 2018-07-27, 12:50Version 1 2018-07-27, 12:50
dataset
posted on 2018-11-17, 17:04authored byLi Liu, Tao Li, Cui-Ting Peng, Chang-Zhen Sun, Chang-Cheng Li, Qing-Jie Xiao, Li-Hui He, Ning-Yu Wang, Ying-Jie Song, Yi-Bo Zhu, Hong Li, Mei Kang, Hong Tang, Xia Xiong, Rui Bao
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.
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.