Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine

Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine

In the Escherichia coli ClpXP protease, a hexameric ClpX ring couples ATP binding and hydrolysis to mechanical protein unfolding and translocation into the ClpP degradation chamber. Rigid-body packing between the small AAA+ domain of each ClpX subunit and the large AAA+ domain of its neighbor stabil...

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Bibliographic Details
Main Authors: Glynn, Steven E. (Contributor), Nager, Andrew Ross (Contributor), Baker, Tania (Contributor), Sauer, Robert T (Author)
Other Authors: Massachusetts Institute of Technology. Department of Biology (Contributor), Whitehead Institute for Biomedical Research (Contributor), Sauer, Robert T. (Contributor)
Format: Article
Language:English
Published: Nature Publishing Group, 2014-01-08T19:07:21Z.
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