The in vivo activity of Tolloid during Drosophila dorsal-ventral patterning is regulated by the differential specificity of its non-catalytic domains in mediating substrate and Collagen IV interaction.
Novel evidence on the molecular determinants of the dual function, anion permeation and substrate transport, of excitatory amino acid transporters opens avenues toward illuminating how these transporters regulate synaptic function and contribute to neurological conditions.
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.
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.
Biochemical analyses and the crystal structure of TtsA reveal fundamental insight into the mechanisms by which this muramidase recognizes its peptidoglycan substrate to facilitate typhoid toxin secretion.
The 26S proteasome lid subcomplex acts as an external scaffold whose interactions with the ATPase motor stabilize the substrate-engagement-competent state, and control conformational changes upon engagement for subsequent degradation steps.