TY - JOUR
T1 - Redox-coupled structural changes of the catalytic a′ domain of protein disulfide isomerase
AU - Inagaki, Koya
AU - Satoh, Tadashi
AU - Yagi-Utsumi, Maho
AU - Le Gulluche, Anne Charlotte
AU - Anzai, Takahiro
AU - Uekusa, Yoshinori
AU - Kamiya, Yukiko
AU - Kato, Koichi
N1 - Funding Information:
We thank Drs. Hisashi Okumura, Satoru G. Itoh, and Takumi Yamaguchi (National Institutes of Natural Sciences) for the valuable discussion and comments on this manuscript and Yukiko Isono (National Institutes of Natural Sciences) for her help in the preparation of the C365S/C368S mutant protein. We also thank Dr. Osamu Asami and Dr. Tsumoto Kajino of Toyota Central Research and Development Laboratory for providing the cDNA of the fungal PDI. This work was supported in part by JSPS KAKENHI (Grant Numbers 24770102 , 25121730 to T.S. and 25102008 to K.K.), by the Okazaki ORION project and by the Nanotechnology Platform Project from the Ministry of Education, Culture, Sports, Science and Technology, Japan.
Publisher Copyright:
© 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
PY - 2015/9/14
Y1 - 2015/9/14
N2 - 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.
AB - 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.
KW - Abbreviations ANS 8-anilino-1-naphthalenesulfonic acid
KW - DTT dithiothreitol
KW - MD molecular dynamics
KW - PDI protein disulfide isomerase
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U2 - 10.1016/j.febslet.2015.07.041
DO - 10.1016/j.febslet.2015.07.041
M3 - Article
C2 - 26272828
AN - SCOPUS:84941417347
SN - 0014-5793
VL - 589
SP - 2690
EP - 2694
JO - FEBS Letters
JF - FEBS Letters
IS - 19
ER -