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., Nager, Andrew Ross, Baker, Tania, Sauer, Robert T
Other Authors: Massachusetts Institute of Technology. Department of Biology
Format: Article
Language:en_US
Published: Nature Publishing Group 2014
Online Access:http://hdl.handle.net/1721.1/83605
https://orcid.org/0000-0002-1719-5399