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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Nature Portfolio
2020
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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) |
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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 |
work_keys_str_mv |
AT sophielmader conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT abrahamlopez conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT jannislawatscheck conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT qiluo conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT danielarutz conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT anapgamizhernandez conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT michaelsattler conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT johannesbuchner conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 AT villerikaila conformationaldynamicsmodulatethecatalyticactivityofthemolecularchaperonehsp90 |
_version_ |
1718383417050005504 |