Sanyasi Chandrasekar, Balakrishnan Susmida Seni, Chinnasamy Thirunavukkarasu, Venugopalan Nagarajan, Kandavelu Palani, Batra-Safferling Renu, Muthuvel Suresh Kumar
Department of Bioinformatics, School of Life Sciences, Pondicherry University, Pondicherry, 605014 India.
Department of Biochemistry and Molecular Biology, School of Life Sciences, Pondicherry University, Pondicherry, 605014 India.
In Silico Pharmacol. 2024 Apr 5;12(1):23. doi: 10.1007/s40203-024-00198-0. eCollection 2024.
The dynamic behavior of Protein Disulfide Isomerase (PDI) in an aqueous solution environment under physiologically active pH has been experimentally verified in this study using Small Angle X-ray Scattering (SAXS) technique. The structural mechanism of dimerization for full-length PDI molecules and co-complex with two renowned substrates has been comprehensively discussed. The structure models obtained from the SAXS data of PDI purified from bovine liver display behavior duality between unaccompanied-enzyme and after engaged with substrates. The analysis of SAXS data revealed that PDI exists as a homo-dimer in the solution environment, and substrate induction provoked its segregation into monomer to enable the enzyme to interact systematically with incoming clients.
The online version contains supplementary material available at 10.1007/s40203-024-00198-0.
在本研究中，使用小角X射线散射（SAXS）技术通过实验验证了蛋白质二硫键异构酶（PDI）在生理活性pH值的水溶液环境中的动态行为。全面讨论了全长PDI分子二聚化以及与两种著名底物形成共复合物的结构机制。从牛肝中纯化的PDI的SAXS数据获得的结构模型显示了未结合酶状态和与底物结合后状态之间的行为二元性。SAXS数据分析表明，PDI在溶液环境中以同型二聚体形式存在，底物诱导促使其分离为单体，以使酶能够与进入的底物进行系统相互作用。
在线版本包含可在10.1007/s40203-024-00198-0获取的补充材料。
