2021年3月11日
Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation.
Scientific reports
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- 巻
- 11
- 号
- 1
- 開始ページ
- 5655
- 終了ページ
- 5655
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/s41598-021-85219-0
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.
- リンク情報
- ID情報
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- DOI : 10.1038/s41598-021-85219-0
- PubMed ID : 33707747
- PubMed Central 記事ID : PMC7952739