7UJ0

ClpAP complex bound to ClpS N-terminal extension, class IIIb

Summary for 7UJ0

• Entry DOI: 10.2210/pdb7uj0/pdb
• EMDB information: 26554 26555 26556 26557 26558 26559
• Descriptor: ATP-dependent Clp protease ATP-binding subunit ClpA, ATP-dependent Clp protease adapter protein ClpS, ATP-dependent Clp protease proteolytic subunit, ... (6 entities in total)
• Functional Keywords: aaa+ protease, adaptor, protein complex, chaperone
• Biological source: Escherichia coli; More
• Total number of polymer chains: 14
• Total formula weight: 682581.19

Authors

Kim, S.,Fei, X.,Sauer, R.T.,Baker, T.A. (deposition date: 2022-03-29, release date: 2022-11-09, Last modification date: 2024-06-12)

Primary citation

Kim, S.,Fei, X.,Sauer, R.T.,Baker, T.A.
AAA+ protease-adaptor structures reveal altered conformations and ring specialization.
Nat.Struct.Mol.Biol., 29:1068-1079, 2022

PubMed Abstract: ClpAP, 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.

PubMed: 36329286
DOI: 10.1038/s41594-022-00850-3

Experimental method

ELECTRON MICROSCOPY (3.26 Å)