6PO3

ClpX-ClpP complex bound to substrate and ATP-gamma-S, class 3

Summary for 6PO3

• Entry DOI: 10.2210/pdb6po3/pdb
• EMDB information: 20408
• Descriptor: ATP-dependent Clp protease ATP-binding subunit ClpX, ATP-dependent Clp protease proteolytic subunit, substrate peptide, ... (5 entities in total)
• Functional Keywords: protein degradation, aaa+ protease complex, chaperone
• Biological source: Escherichia coli; More
• Total number of polymer chains: 14
• Total formula weight: 405209.55

Authors

Fei, X.,Jenni, S.,Harrison, S.C.,Sauer, R.T. (deposition date: 2019-07-03, release date: 2020-03-11, Last modification date: 2024-03-20)

Primary citation

Fei, X.,Bell, T.A.,Jenni, S.,Stinson, B.M.,Baker, T.A.,Harrison, S.C.,Sauer, R.T.
Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate.
Elife, 9:-, 2020

PubMed Abstract: ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and translocates specific protein substrates into the degradation chamber of ClpP. We present cryo-EM studies of the enzyme that show how asymmetric hexameric rings of ClpX bind symmetric heptameric rings of ClpP and interact with protein substrates. Subunits in the ClpX hexamer assume a spiral conformation and interact with two-residue segments of substrate in the axial channel, as observed for other AAA+ proteases and protein-remodeling machines. Strictly sequential models of ATP hydrolysis and a power stroke that moves two residues of the substrate per translocation step have been inferred from these structural features for other AAA+ unfoldases, but biochemical and single-molecule biophysical studies indicate that ClpXP operates by a probabilistic mechanism in which five to eight residues are translocated for each ATP hydrolyzed. We propose structure-based models that could account for the functional results.

PubMed: 32108573
DOI: 10.7554/eLife.52774

Experimental method

ELECTRON MICROSCOPY (4.28 Å)