Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation

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 differ...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Aya Okuda, Masahiro Shimizu, Ken Morishima, Rintaro Inoue, Nobuhiro Sato, Reiko Urade, Masaaki Sugiyama
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ad41e2aa6cd3420e869018a7efea4c15
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:ad41e2aa6cd3420e869018a7efea4c15
record_format	dspace
spelling	oai:doaj.org-article:ad41e2aa6cd3420e869018a7efea4c152021-12-02T13:34:57ZSolution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation10.1038/s41598-021-85219-02045-2322https://doaj.org/article/ad41e2aa6cd3420e869018a7efea4c152021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-85219-0https://doaj.org/toc/2045-2322Abstract 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.Aya OkudaMasahiro ShimizuKen MorishimaRintaro InoueNobuhiro SatoReiko UradeMasaaki SugiyamaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Aya Okuda Masahiro Shimizu Ken Morishima Rintaro Inoue Nobuhiro Sato Reiko Urade Masaaki Sugiyama Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation
description	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.
format	article
author	Aya Okuda Masahiro Shimizu Ken Morishima Rintaro Inoue Nobuhiro Sato Reiko Urade Masaaki Sugiyama
author_facet	Aya Okuda Masahiro Shimizu Ken Morishima Rintaro Inoue Nobuhiro Sato Reiko Urade Masaaki Sugiyama
author_sort	Aya Okuda
title	Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation
title_short	Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation
title_full	Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation
title_fullStr	Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation
title_full_unstemmed	Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation
title_sort	solution structure of multi-domain protein er-60 studied by aggregation-free saxs and coarse-grained-md simulation
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ad41e2aa6cd3420e869018a7efea4c15
work_keys_str_mv	AT ayaokuda solutionstructureofmultidomainproteiner60studiedbyaggregationfreesaxsandcoarsegrainedmdsimulation AT masahiroshimizu solutionstructureofmultidomainproteiner60studiedbyaggregationfreesaxsandcoarsegrainedmdsimulation AT kenmorishima solutionstructureofmultidomainproteiner60studiedbyaggregationfreesaxsandcoarsegrainedmdsimulation AT rintaroinoue solutionstructureofmultidomainproteiner60studiedbyaggregationfreesaxsandcoarsegrainedmdsimulation AT nobuhirosato solutionstructureofmultidomainproteiner60studiedbyaggregationfreesaxsandcoarsegrainedmdsimulation AT reikourade solutionstructureofmultidomainproteiner60studiedbyaggregationfreesaxsandcoarsegrainedmdsimulation AT masaakisugiyama solutionstructureofmultidomainproteiner60studiedbyaggregationfreesaxsandcoarsegrainedmdsimulation
_version_	1718392756601094144

Solution structure of multi-domain protein ER-60 studied by aggregation-free SAXS and coarse-grained-MD simulation

Ejemplares similares