Msp1, a membrane-integral AAA ATPase at mitochondria and peroxisomes, selectively recognizes uncomplexed substrate molecules in vivo while avoiding substrates stabilized by binding partners.

The AAA+ protein unfolding motor ClpX grips substrates with the uppermost part of its substrate-binding pore, and requires interactions with hydrophobic amino acid side chains to operate with optimal efficiency.

TRIP13 inactivates the spindle assembly checkpoint by converting MAD2 from its active ‘closed’ state to its inactive ‘open’ state.

A mitochondrial membrane-bound protein ATAD1 uses conserved structural elements to remove mislocalized membrane proteins from the outer mitochondrial membrane, achieving proper cell organization.

Msp1 recruits substrates at the open seam of the spiral oligomer and extracts them with functionally adapted elements.

The N-terminal domains enable Lon protease to discriminate and capture selected protein species for degradation by exposed hydrophobic patches and flexible linkages to the hexameric core complex.

The high-resolution structure of Rea1, an essential ribosome maturation factor in Saccharomyces cerevisiae, explains how the ATPase domain is regulated and reveals the linker domain, the mechanical element carrying out ribosome remodeling.

Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.

Electron-cryomicroscopy structures of the supercomplex of NSF, αSNAP, and neuronal SNAREs in the presence of ATP under non-hydrolyzing conditions at 3.9 Å resolution reveal interactions between the N-terminal residues of SNAP-25 and NSF.

A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.