Redox-coupled structural changes of the catalytic a′ domain of protein disulfide isomerase

Koya Inagaki, Tadashi Satoh, Maho Yagi-Utsumi, Anne Charlotte Le Gulluche, Takahiro Anzai, Yoshinori Uekusa, Yukiko Kamiya, Koichi Kato

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Protein disulfide isomerase functions as a folding catalyst in the endoplasmic reticulum. Its b′ and a′ domains provide substrate-binding sites and undergo a redox-dependent domain rearrangement coupled to an open-closed structural change. Here we determined the first solution structure of the a′ domain in its oxidized form and thereby demonstrate that oxidation of the a′ domain induces significant conformational changes not only in the vicinity of the active site but also in the distal b′-interfacial segment. Based on these findings, we propose that this conformational transition triggers the domain segregation coupled with the exposure of the hydrophobic surface.

Original languageEnglish
Pages (from-to)2690-2694
Number of pages5
JournalFEBS Letters
Volume589
Issue number19
DOIs
Publication statusPublished - 2015 Sep 14
Externally publishedYes

Keywords

  • Abbreviations ANS 8-anilino-1-naphthalenesulfonic acid
  • DTT dithiothreitol
  • MD molecular dynamics
  • PDI protein disulfide isomerase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Inagaki, K., Satoh, T., Yagi-Utsumi, M., Le Gulluche, A. C., Anzai, T., Uekusa, Y., Kamiya, Y., & Kato, K. (2015). Redox-coupled structural changes of the catalytic a′ domain of protein disulfide isomerase. FEBS Letters, 589(19), 2690-2694. https://doi.org/10.1016/j.febslet.2015.07.041