Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX
The hexameric AAA+ ring of Escherichia coli ClpX, an ATP-dependent machine for protein unfolding and translocation, functions with the ClpP peptidase to degrade target substrates. For efficient function, ClpX subunits must switch between nucleotide-loadable (L) and nucleotide-unloadable (U) conforma...
Main Authors: | , , , , |
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Other Authors: | |
Format: | Article |
Language: | en_US |
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Nature Publishing Group
2017
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Online Access: | http://hdl.handle.net/1721.1/108783 https://orcid.org/0000-0002-7390-3580 https://orcid.org/0000-0002-9309-8662 https://orcid.org/0000-0002-1719-5399 |