Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique

被引：0
作者：
Chandrasekar Sanyasi
Susmida Seni Balakrishnan
Thirunavukkarasu Chinnasamy
Nagarajan Venugopalan
Palani Kandavelu
Renu Batra-Safferling
Suresh Kumar Muthuvel
机构：
[1] Pondicherry University,Department of Bioinformatics, School of Life Sciences
[2] Pondicherry University,Department of Biochemistry and Molecular Biology, School of Life Sciences
[3] Argonne National Laboratory,GMCA Structural Biology Facility, X
[4] University of Georgia,Ray Science Division
[5] Forschungszentrum Jülich,SER
来源：
In Silico Pharmacology | / 12卷 / 1期
关键词：
Protein Disulfide Isomerase; Bovine pancreatic trypsin inhibitor; Ribonuclease; Small-angle X-ray scattering; Ab-initio modeling; Ensemble Optimization Method;
D O I：
10.1007/s40203-024-00198-0
中图分类号：
学科分类号：
摘要：
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.
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