Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90

The chaperone Hsp90 uses the free energy from ATP hydrolysis to control the folding of client proteins in eukaryotic cells. Here the authors provide mechanistic insights into how its catalytic activity is coupled to conformational changes by combining large-scale molecular simulations with NMR, FRET...

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Autores principales: Sophie L. Mader, Abraham Lopez, Jannis Lawatscheck, Qi Luo, Daniel A. Rutz, Ana P. Gamiz-Hernandez, Michael Sattler, Johannes Buchner, Ville R. I. Kaila
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Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/b87ff0e02f1548cc99bb836c5ec50ea7
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spelling oai:doaj.org-article:b87ff0e02f1548cc99bb836c5ec50ea72021-12-02T16:49:14ZConformational dynamics modulate the catalytic activity of the molecular chaperone Hsp9010.1038/s41467-020-15050-02041-1723https://doaj.org/article/b87ff0e02f1548cc99bb836c5ec50ea72020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15050-0https://doaj.org/toc/2041-1723The chaperone Hsp90 uses the free energy from ATP hydrolysis to control the folding of client proteins in eukaryotic cells. Here the authors provide mechanistic insights into how its catalytic activity is coupled to conformational changes by combining large-scale molecular simulations with NMR, FRET and SAXS experiments.Sophie L. MaderAbraham LopezJannis LawatscheckQi LuoDaniel A. RutzAna P. Gamiz-HernandezMichael SattlerJohannes BuchnerVille R. I. KailaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Sophie L. Mader
Abraham Lopez
Jannis Lawatscheck
Qi Luo
Daniel A. Rutz
Ana P. Gamiz-Hernandez
Michael Sattler
Johannes Buchner
Ville R. I. Kaila
Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
description The chaperone Hsp90 uses the free energy from ATP hydrolysis to control the folding of client proteins in eukaryotic cells. Here the authors provide mechanistic insights into how its catalytic activity is coupled to conformational changes by combining large-scale molecular simulations with NMR, FRET and SAXS experiments.
format article
author Sophie L. Mader
Abraham Lopez
Jannis Lawatscheck
Qi Luo
Daniel A. Rutz
Ana P. Gamiz-Hernandez
Michael Sattler
Johannes Buchner
Ville R. I. Kaila
author_facet Sophie L. Mader
Abraham Lopez
Jannis Lawatscheck
Qi Luo
Daniel A. Rutz
Ana P. Gamiz-Hernandez
Michael Sattler
Johannes Buchner
Ville R. I. Kaila
author_sort Sophie L. Mader
title Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
title_short Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
title_full Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
title_fullStr Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
title_full_unstemmed Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
title_sort conformational dynamics modulate the catalytic activity of the molecular chaperone hsp90
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/b87ff0e02f1548cc99bb836c5ec50ea7
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