Downloads: 38

Files in This Item:
File Description SizeFormat 
s41598-021-85219-0.pdf2.7 MBAdobe PDFView/Open
Title: Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation
Authors: Okuda, Aya  kyouindb  KAKEN_id  orcid (unconfirmed)
Shimizu, Masahiro
Morishima, Ken  kyouindb  KAKEN_id  orcid (unconfirmed)
Inoue, Rintaro  kyouindb  KAKEN_id
Sato, Nobuhiro  kyouindb  KAKEN_id  orcid (unconfirmed)
Urade, Reiko  kyouindb  KAKEN_id  orcid (unconfirmed)
Sugiyama, Masaaki
Author's alias: 奥田, 綾
清水, 将裕
守島, 健
井上, 倫太郎
佐藤, 信浩
裏出, 令子
杉山, 正明
Keywords: SAXS
Structural biology
Issue Date: 11-Mar-2021
Publisher: Springer Nature
Journal title: Scientific Reports
Volume: 11
Thesis number: 5655
Abstract: Multi-domain proteins (MDPs) show a variety of domain conformations under physiological conditions, regulating their functions through such conformational changes. One of the typical MDPs, ER-60 which is a protein folding enzyme, has a U-shape with four domains and is thought to have different domain conformations in solution depending on the redox state at the active centres of the edge domains. In this work, an aggregation-free small-angle X-ray scattering revealed that the structures of oxidized and reduced ER-60 in solution are different from each other and are also different from those in the crystal. Furthermore, structural modelling with coarse-grained molecular dynamics simulation indicated that the distance between the two edge domains of oxidized ER-60 is longer than that of reduced ER-60. In addition, one of the edge domains has a more flexible conformation than the other.
Rights: © The Author(s) 2021. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit
DOI(Published Version): 10.1038/s41598-021-85219-0
PubMed ID: 33707747
Appears in Collections:Journal Articles

Show full item record

Export to RefWorks

Export Format: 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.