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pH dependent conformational changes in the bacterial Hsp90 reveal a Grp94-like conformation at pH6 that is highly active for suppression of citrate synthase aggregation
The molecular chaperone Hsp90 depends upon large conformational rearrangements for its function. One driving force for these rearrangements is the intrinsic ATPase activity of Hsp90, as seen with other chaperones. However, unlike other chaperones, structural and kinetic studies have shown that the A...
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| Main Authors: | , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2009
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2735500/ https://ncbi.nlm.nih.gov/pubmed/19427321 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2009.04.080 |
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