Atomic structures suggest a novel mechanism for the regulation of mRNA transcription and capping in dsRNA viruses.

In potassium-dependent NTPases, insertion of the activating potassium ion into the active site leads to rotation of the gamma-phosphate yielding a near-eclipsed, catalytically productive conformation of the triphosphate chain.

The GTPase Nog1 orchestrates stalk assembly, peptidyl transferase centre maturation and polypeptide exit tunnel quality control.

Relocation of Rab, Ras and Rho family GTPases to the surface of mitochondria enables efficient identification of their effectors, exchange factors and GAPs by proximity biotinylation.

Coordinate control of lysosomal v-ATPase subunits and biogenesis factor TFEB by miR-1 identifies a key regulatory axis with strong links to age-related proteotoxic disease.

Small Rho GTPases confer up- and downregulation in mammalian plexin signaling by differential interactions with cell membrane.

Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H⁺ translocation in the V_o membrane domain.

Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.

Reengineering the nucleotide-binding pocket of an extant ATPase to restore ancestral GTPase activity revealed an ATP-dependent intermediate required for function and suggested why the protein evolved to use ATP.

A biochemical approach unveils the overall shape of a subclass of heavy-metal transporting pumps, thereby shedding light on principle molecular determinants linked to the transport mechanism of these elusive machines, information that is critical well beyond basic science.