Cryo-EM reveals the regulation of RUVBL1 and RUVBL2 AAA-ATPases by DHX34, a helicase involved in nonsense-mediated mRNA decay (NMD), and suggests mechanisms for how RUVBL1 and RUVBL2 function in NMD.

Probing the DNA motor SpoIIIE at the single-molecule level has revealed its force-generating step, rich translocation dynamics during motor operation and a novel, bi-phasic mechanical response to opposing force.

The subunits of the SpoIIIE motor contact the 5'→3' strand of DNA in sequence to rapidly translocate the DNA across a membrane.

LAP1 adopts an AAA+ like fold that, while unable to bind nucleotide, can enhance ATPase activity in the neighboring TorsinA protomer in an unusual heterohexameric ring, via an arginine finger.

The Mcm2-7 motor unwinds DNA using an approach distinct from that of superfamily III helicases, and accesses multiple ring configurations and assembly states during the initiation of DNA replication.

Empirical energy landscape allows simulating the structural dynamics of the proteasomal ATPase complex, which yields predictions that are widely consistent with experimental observations and reveals the functional mechanism of the proteasome in substrate degradation.

RNF213 is a giant E3 ligase with a dynein-like core and a unique ubiquitination mechanism that proceeds in a RING-independent manner and is linked with the Moyamoya disease.

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

Single-molecule F₁F_O studies show mutation-dependent pKa changes of both F_O half-channels, and proton translocation-dependent 11° ATP synthase-direction sub-steps, which support a Grotthuss proton transfer-dependent two-step F_O torque generating mechanism.

In Escherichia coli structural maintenance of chromosomes (SMC) complex, MukBEF, a dimeric MukF kleisin binds and activates MukB SMC ATPases through two independent interfaces provided by distinct MukF N- and C-terminal domains.