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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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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
2014
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| Assuntos: | |
| Acceso en liña: | 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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