6WR2
ClpP and ClpX IGF loop in ClpX-ClpP complex bound to ssrA tagged GFP
Summary for 6WR2
| Entry DOI | 10.2210/pdb6wr2/pdb |
| EMDB information | 21875 |
| Descriptor | ATP-dependent Clp protease ATP-binding subunit ClpX, ATP-dependent Clp protease proteolytic subunit (3 entities in total) |
| Functional Keywords | protein degradation, aaa+ protease complex, chaperone |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 20 |
| Total formula weight | 582699.04 |
| Authors | Fei, X.,Sauer, R.T. (deposition date: 2020-04-29, release date: 2020-11-04, Last modification date: 2024-03-06) |
| Primary citation | Fei, X.,Bell, T.A.,Barkow, S.R.,Baker, T.A.,Sauer, R.T. Structural basis of ClpXP recognition and unfolding of ssrA-tagged substrates. Elife, 9:-, 2020 Cited by PubMed Abstract: When ribosomes fail to complete normal translation, all cells have mechanisms to ensure degradation of the resulting partial proteins to safeguard proteome integrity. In and other eubacteria, the tmRNA system rescues stalled ribosomes and adds an ssrA tag or degron to the C-terminus of the incomplete protein, which directs degradation by the AAA+ ClpXP protease. Here, we present cryo-EM structures of ClpXP bound to the ssrA degron. C-terminal residues of the ssrA degron initially bind in the top of an otherwise closed ClpX axial channel and subsequently move deeper into an open channel. For short-degron protein substrates, we show that unfolding can occur directly from the initial closed-channel complex. For longer degron substrates, our studies illuminate how ClpXP transitions from specific recognition into a nonspecific unfolding and translocation machine. Many AAA+ proteases and protein-remodeling motors are likely to employ similar multistep recognition and engagement strategies. PubMed: 33089779DOI: 10.7554/eLife.61496 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.88 Å) |
Structure validation
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