Cryo-electron microscopy structures show how the clinically used antimicrobial fidaxomicin binds and inhibits Mycobacterium tuberculosis RNA polymerase by acting like a doorstop to jam the enzyme in an open conformation via the general transcription factor RbpA.
The first crystal structure of an active plant asparaginyl endopeptidase reveals a tetrahedral intermediate state in its active site, which may help to explain why these enzymes have been independently recruited to perform peptide macrocyclization.
Individual nonmuscle myosin 2 filaments in cells may differ their mechanical and kinetic properties depending on the myosin paralog composition giving the cells a mechanism for fine tuning the output of a given nonmuscle myosin filament.
Biomimetic nanopores reveal that the sequence-dependent spatial distribution of intrinsically disordered proteins plays a crucial role in establishing the selective permeability barrier of the nuclear pore complex.
Cryo-electron microscopy structures of human ribonucleotide reductase reveal molecular details of substrate selection and allosteric inhibition through assembly of its large subunit into a ring that excludes its small subunit.
Quantitative microscopy and theory show that the size of Xenopus laevis egg extract spindles is controlled by a spatially-regulated autocatalytic growth mechanism driven by microtubule-stimulated microtubule nucleation.
The primary cilia polycystin proteins, polycystin-1 and polycystin-2, affect cilia length in the kidney collecting duct epithelia, but only polycystin-2 is required for the functional ion channel in this organelle.