Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1

Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1

Hsp90 is a homodimeric ATP-dependent molecular chaperone that remodels its substrate ‘client’ proteins, facilitating their folding and activating them for biological function. Despite decades of research, the mechanism connecting ATP hydrolysis and chaperone function remains elusive. Particularly pu...

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Bibliographic Details
Main Authors: Daniel Elnatan, Miguel Betegon, Yanxin Liu, Theresa Ramelot, Michael A Kennedy, David A Agard
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2017-07-01
Series:eLife
Subjects:
Hsp90
TRAP1
chaperone
ATP hydrolysis
homodimer
asymmetry
Online Access:https://elifesciences.org/articles/25235

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