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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Detalles Bibliográficos
Autores principales: Elnatan, Daniel, Betegon, Miguel, Liu, Yanxin, Ramelot, Theresa, Kennedy, Michael A, Agard, David A
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2017
Materias:
Biochemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5550277/
https://www.ncbi.nlm.nih.gov/pubmed/28742020
http://dx.doi.org/10.7554/eLife.25235

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5550277/
https://www.ncbi.nlm.nih.gov/pubmed/28742020
http://dx.doi.org/10.7554/eLife.25235

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