AAA+ protease-adaptor structures reveal altered conformations and ring specialization
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s41594-022-00850-3.pdf
Description
Published version
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9.79 MB
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Checksum (MD5)
7edd8dffcfddf3a4fcd572db370a4fd8
Author(s)
Kim, Sora
Fei, Xue
Sauer, Robert T
Baker, Tania A
Date Issued
November 2022
Journal
Nature Structural & Molecular Biology
Publisher
Springer Science and Business Media LLC
Citation
Kim, Sora, Fei, Xue, Sauer, Robert T and Baker, Tania A. 2022. "AAA+ protease-adaptor structures reveal altered conformations and ring specialization." Nature Structural & Molecular Biology, 29 (11).
Version
Final published version
Abstract
AbstractClpAP, a two-ring AAA+ protease, degrades N-end-rule proteins bound by the ClpS adaptor. Here we present high-resolution cryo-EM structures of Escherichia coli ClpAPS complexes, showing how ClpA pore loops interact with the ClpS N-terminal extension (NTE), which is normally intrinsically disordered. In two classes, the NTE is bound by a spiral of pore-1 and pore-2 loops in a manner similar to substrate-polypeptide binding by many AAA+ unfoldases. Kinetic studies reveal that pore-2 loops of the ClpA D1 ring catalyze the protein remodeling required for substrate delivery by ClpS. In a third class, D2 pore-1 loops are rotated, tucked away from the channel and do not bind the NTE, demonstrating asymmetry in engagement by the D1 and D2 rings. These studies show additional structures and functions for key AAA+ elements. Pore-loop tucking may be used broadly by AAA+ unfoldases, for example, during enzyme pausing/unloading.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution 4.0 International license
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DOI of Published Version
https://doi.org/10.1038/s41594-022-00850-3
