Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
The cryo-EM structure and functional analyses of oxytocin bound to its receptor reveal a Mg2+ coordination complex in the binding pocket and find that the identity of a single residue determines whether a vasopressin/oxytocin family receptor requires Mg2+ as a cofactor.
HDX–MS analysis reveals the SARS-CoV-2 spike ectodomain reversibly samples an open-trimer conformation that reveals epitopes for a pan-coronavirus antibody; interconversion with the prefusion conformation is modulated by temperature, ACE2 receptor binding, and sequence variants.
Cryo-EM structures of somatostatin 14- and octreotide-bound somatostatin receptor 2 reveal a flexible extracellular domain for recognizing different ligands and, together with functional assays, identify the basis of SSTR subtype selectivity.
Arlt et al. report a structure of yeast seipin, a lipid droplet formation protein, and suggest that it forms a flexible, oligomeric cage in the endoplasmic reticulum membrane, enabling triacylglycerol phase separation, lipid droplet growth and budding toward the cytoplasm.
The authors solve the cryo-EM structure of nucleotide-free Chd1 bound to a nucleosome to dissect how Chd1 shifts DNA onto the histone core, and also report that recognition of the acidic patch by Chd1 blocks action of competing chromatin remodelers.
Activation of the Tn7 transposase depends on the Tn7-encoded AAA+ ATPase adaptor, TnsC. A new cryo-EM structure reveals how TnsC targets DNA sequences between target and insertion sites to restrict insertion events to control sequence-specific transposon insertion.
NHA2 exchanges sodium ions for protons across cell membranes, and its activity is linked to the pathogenesis of diabetes mellitus and essential hypertension in humans. Drew et al. report the cryo-EM structure of NHA2 in detergent and nanodiscs.
Growing evidence suggests that many ribosome-targeting antibiotics inhibit protein synthesis context specifically, which has important implications for drug development. New work reveals the structural basis of context-specific action of the classic translation inhibitor chloramphenicol and the oxazolidinones linezolid and radezolid.
The authors solve structures of the bacterial ribosome bound to the peptidyl transferase center targeting antibiotic chloramphenicol with adjacent growing peptide chains to explain the context-specificity of action of this antibiotic.
The authors determine the cryo-EM structures of prokaryotic ribosomes with the oxazolidinone antibiotics linezolid and radezolid bound to the peptidyl transferase center with an adjacent growing nascent peptide chain, providing an explanation for their context-specific action.
Cryo-EM structures of the human pentameric glycosylphosphatidylinositol transamidase (GPIT) complex reveal its subunit assembly and its catalytic and GPI-binding sites.
Cryo-EM structures of the porcine respiratory complex I reveal how Q10 is bound and reduced in the Q chamber comprising four different Q10-binding sites. A ‘two-Q’ model is proposed for the coupling mechanism of complex I.
Courtney et al. found that the C-terminal amphipathic helix of a presynaptic protein, complexin, can dramatically remodel phospholipid bilayers. This activity enables complexin to increase the size and stability of SNARE-mediated fusion pores.
Genetic and genome-wide analysis of a catalytically deficient SETDB1-like enzyme, MET-2, in Caenorhabditiselegans reveals that MET-2 promotes transcriptional silencing and fertility through both H3K9 methylation and focus formation, which blocks histone acetylation.