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Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism

While structural symmetry is a prevailing feature of homo-oligomeric proteins, asymmetry provides unique mechanistic opportunities. We present the crystal structure of full-length TRAP1, the mitochondrial Hsp90 molecular chaperone, in a catalytically active closed state. The TRAP1 homodimer adopts a...

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Detalhes bibliográficos
Main Authors: Lavery, Laura A., Partridge, James R., Ramelot, Theresa A., Elnatan, Daniel, Kennedy, Michael A., Agard, David A.
Formato: Artigo
Idioma:Inglês
Publicado em: 2014
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3947485/
https://ncbi.nlm.nih.gov/pubmed/24462206
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2013.12.023
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