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タイトル: | Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation |
著者: | Okuda, Aya https://orcid.org/0000-0002-6222-8364 (unconfirmed) Shimizu, Masahiro Morishima, Ken https://orcid.org/0000-0003-1091-3850 (unconfirmed) Inoue, Rintaro Sato, Nobuhiro https://orcid.org/0000-0002-6960-6567 (unconfirmed) Urade, Reiko https://orcid.org/0000-0002-9232-6176 (unconfirmed) Sugiyama, Masaaki |
著者名の別形: | 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 |
キーワード: | SAXS Structural biology |
発行日: | 11-Mar-2021 |
出版者: | Springer Nature |
誌名: | Scientific Reports |
巻: | 11 |
論文番号: | 5655 |
抄録: | 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. |
著作権等: | © 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 http://creativecommons.org/licenses/by/4.0/. |
URI: | http://hdl.handle.net/2433/262260 |
DOI(出版社版): | 10.1038/s41598-021-85219-0 |
PubMed ID: | 33707747 |
出現コレクション: | 学術雑誌掲載論文等 |
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