The crystal structure of a ternary complex of a TonB-dependent transporter containing a signalling domain, bound to siderophore as well as TonB, provides mechanistic insights into siderophore uptake and signalling.
A mitochondrial membrane-bound protein ATAD1 uses conserved structural elements to remove mislocalized membrane proteins from the outer mitochondrial membrane, achieving proper cell organization.
The structure of gp41with its membrane anchors highlights the flexible linkage of the transmembrane regions and the fuson peptides, which generates an asymmetric conformation, a potential target of MPER bNAbs.
Florian Bleffert, Joachim Granzin ... Filip Kovacic
Membrane homeostasis in bacteria relies on the controlled degradation of endogenous phospholipids by intracellular phospholipases A, however their structures and catalytic mechanism are still poorly understood.
Diana C Rodriguez Camargo, Kyle J Korshavn ... Ayyalusamy Ramamoorthy
The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.
Katharina van Pee, Alexander Neuhaus ... Özkan Yildiz
The near-atomic cryoEM pore complex structure of pneumolysin, the main virulence factor of Streptococcus pneumoniae, shows how the individual domains rearrange during the pore formation.
The crystal structure of human WIPI2 bound to the ATG16L1 WIPI2-interacting region, combined with in vitro reconstitution and cellular autophagy assays, shows how the LC3 lipidation machinery is recruited in autophagy initiation.
Lakshmi E Miller-Vedam, Bastian Bräuning ... Jonathan S Weissman
Structure-function characterization of the EMC's cytoplasmic, transmembrane, and lumenal domains reveal features critical for terminal helix insertion and a specialized role for the lumenal domain in polytopic membrane protein biogenesis.
The structure of a bivalent double-knot tarantula toxin bound to the outer pore of the capsaicin receptor reveals a novel mode of toxin-channel recognition that has important implications for thermosensation.