Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding

Proteolytic AAA+ unfoldases use ATP hydrolysis to power conformational changes that mechanically denature protein substrates and then translocate the polypeptide through a narrow pore into a degradation chamber. We show that a tyrosine in a pore loop of the hexameric ClpX unfoldase links ATP hydroly...

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Detalles Bibliográficos
Autores principales: Martin, Andreas, Baker, Tania A., Sauer, Robert T.
Formato: Texto
Lenguaje:English
Publicado: 2008
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2610342/
https://www.ncbi.nlm.nih.gov/pubmed/18931677
http://dx.doi.org/10.1038/nsmb.1503

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2610342/
https://www.ncbi.nlm.nih.gov/pubmed/18931677
http://dx.doi.org/10.1038/nsmb.1503

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