Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.
The structure of the catalytic core of the N6-methyladenosine RNA methyltransferase complex METTL3-METTL14 reveals that METTL3 is the catalytic subunit, while METTL14 plays non-catalytic roles in substrate recognition and in maintaining complex integrity.
Phosphorylation of Aurora A does not trigger a population shift to the active state as previously thought, but instead switches the kinase on by tuning the structure and dynamics of a dynamically sampled subpopulation.
The SHIP2 inositol phosphatase is an important upstream regulator of the Akt signaling pathway, which requires a catalytic core formed by the phosphatase domain tightly packed to a C2 domain for its function.
Structures of active and inactive conformations of a PP2C family phosphatase reveal a conserved switch that controls enzymatic activity and point to an unexpected relationship between phosphatases and proteasomal proteases.
Structural research, supplemented by biochemical experiments and enzymatic assays, unravels the sequence-dependent molecular mechanism by which SETD3 recognizes β-actin and methylates His73 of β-actin.
DNA-bound crystal structures of an essential Xer site-specific recombinase from the bacterium Helicobacter pylori reveal how large conformational changes initiate the untangling of chromosomes upon cell division.
The common post-translational modification trans-4-hydroxy-L-proline is reversed by gut microbes with the help of hydroxyproline dehydratase (HypD), an enzyme that performs a radical chemical mechanism.