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

@inproceedings{Elnatan2017SymmetryBA,
  title={Symmetry broken and rebroken during the ATP hydrolysis cycle of the mitochondrial Hsp90 TRAP1},
  author={Daniel Elnatan and Miguel Betegon and Yanxin Liu and Theresa A. Ramelot and Michael A Kennedy and David A. Agard},
  booktitle={eLife},
  year={2017}
}
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 puzzling has been the apparent lack of cooperativity in hydrolysis of the ATP in each protomer. A crystal structure of the mitochondrial Hsp90, TRAP1, revealed that the catalytically active state is… CONTINUE READING
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