| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10802549 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2012 | 14 Pages |
Abstract
⺠Ring hexamers of ClpX unfold and then translocate proteins into ClpP for degradation. ⺠A narrow pore restricts ClpP activity unless ClpX/ClpA or acyldepsipeptides bind. ⺠ClpX recognizes peptide tags or degrons in protein substrates and adaptor proteins. ⺠Asymmetric ATP hydrolysis by one ClpX subunit powers mechanical protein unfolding. ⺠Crystallography and single-molecule results reveal detailed aspects of mechanism.
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Authors
Tania A. Baker, Robert T. Sauer,