Structural and molecular dynamic studies of Pseudomonas aeruginosa OdaA reveal the regulation role of a C-terminal hinge element.
Structural and molecular dynamic studies of Pseudomonas aeruginosa OdaA reveal the regulation role of a C-terminal hinge element.
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铜绿假单胞菌 OdaA 的结构和分子动力学研究揭示了 C 末端铰链元件的调节作用。
DOI：
10.1016/j.bbagen.2020.129756
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Bao Rui
中科院分区：
文献类型：
--
作者：
Zhao Ning-Lin;Zhang Qian-Qian;Zhao Chang;Liu Li;Li Tao;Li Chang-Cheng;He Li-Hui;Zhu Yi-Bo;Song Ying-Jie;Liu Huan-Xiang;Bao Rui
BackgroundCrotonase superfamily members exhibit great catalytic diversity towards various acyl-CoA substrates. A common CoA moiety binding pattern is usually observed in this family, understanding the substrate-binding mechanism would facilitate the rational engineering of crotonases for improved properties.MethodsWe applied X-ray crystallography to investigate a putative enoyl-CoA hydratase/isomerase OdaA inPseudomonas aeruginosa. Thermal shift assay (TSA) were performed to explore the binding of OdaA with CoA thioester substrates. Furthermore, we performed molecular dynamics (MD) simulations to elucidate the dynamics of its CoA-binding site.ResultsWe solved the crystal structures of the apo and CoA-bound OdaA. Thermal shift assay (TSA) showed that CoA thioester substrates bind to OdaA with a different degree. MD simulations demonstrated that the C-terminal alpha helix underwent a structural transition and a hinge region would associate with this conformational change.ConclusionsTSA in combination with MD simulations elucidate that the dynamics of C-terminal alpha helix in CoA-binding, and a hinge region play an important role in conformational change.General significanceThose results help to extend our knowledge about the nature of crotonases and would be informative for future mechanistic studies and industry applications.
