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.
Structural and functional studies reveal how Newcastle disease virus nucleocapsid protects its viral genome through a self-capping mechanism, which is important for new antiviral drug design.
In situ structural analysis of bacterial flagellar motor in the Lyme disease spirochete reveals novel conformational change driven by proton motive force.
TMEM206 proteins are identified as constituting the pore of the widely expressed acid-activated chloride channel PAORAC/ASOR, which is important in acid toxicity.
Detection of unbinding transitional states in the charybdotoxin first-order dissociation from a Kv-channel reveals that the bound neurotoxin wobbles, suggesting diverse intermediates and dissociation pathways in this protein–protein interaction.
The cryo-EM structure and functional characterization of the chloride-selective ion transporter Slc26a9 defines its oligomeric architecture and transport mechanism.
Hydrogen-deuterium exchange mass spectrometry reveals nucleotide-driven conformational regulation of Sec protein-channel to help impose directionality for protein transport through the Sec complex.
