Journal Article

FZJ-2024-03003

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Insights on the dynamic behavior of protein disulfide isomerase in the solution environment through the SAXS technique

Sanyasi, C. ; Balakrishnan, S. S. ; Chinnasamy, T. ; Venugopalan, N. ; Kandavelu, P. ; Batra-Safferling, R.FZJ* ; Muthuvel, S. K. (Corresponding author)

2024
SpringerOpen Heidelberg [u.a.]

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Please use a persistent id in citations: doi:10.1007/s40203-024-00198-0

Abstract: 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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Contributing Institute(s):

1. Strukturbiochemie (IBI-7)

Research Program(s):

1. 5241 - Molecular Information Processing in Cellular Systems (POF4-524) (POF4-524)

Appears in the scientific report 2024

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Database coverage:
; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; DEAL Springer ; DEAL Springer ; Ebsco Academic Search

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