Volume 28 Issue 8, August 2021

Atomic force microscopy (AFM) is unique in visualizing functional biomolecules in aqueous solution at ~1 nm resolution. By borrowing localization methods from fluorescence microscopy, AFM has been shown to discern structural domains that may be separated by only a few Ångströms.

The folding of ribosomal RNAs is central to the biogenesis of the mitoribosome and is a complex, stepwise process. Five recent cryo-EM studies detail the late steps of the folding and maturation of the human mitoribosomal large subunit RNA that forms the catalytic core of the ribosome: the peptidyl transferase center (PTC).

Dimeric multidomain metabotropic glutamate receptors modulate excitatory neurotransmission in the brain. Three articles in Nature provide unparalleled insights into how glutamate and drug-like molecules induce asymmetric shape changes in these multidomain receptors to promote coupling to an intracellular protein partner.

Hi-C analyses of engineered Bacillus subtilis strains with defined SMC loading sites and 3D polymer simulations indicate that SMC complex encounters on the same DNA are resolved via bypassing in vivo.

Cryo-EM structures of CRISPR–CasΦ, a small RNA-guided enzyme unique to bacteriophages, reveal how CasΦ binds to and cleaves DNA, paving the way for engineering of improved CasΦ variants for diagnostics and genome-editing applications.

Identification of the tumor suppressor FLCN as an intracellular inhibitor of LDHA and a regulator of the Warburg effect provides a new paradigm for the regulation of glycolysis.

A crystal structure of the MEILB2–BRCA2 complex critical for BRCA2 recruitment to meiotic recombination sites shows the complex adopts a new 4:2 geometry that dictates the localization of both proteins in cells.

Crystallographic, electron microscopy and biophysical studies reveal how the synaptonemal complex component SYCE2-TEX12 undergoes self-assembly into fibrous supramolecular structures that mediate homologous chromosome synapsis in meiosis.

A cryo-EM structure of the active human melatonin receptor in complex with G_i reveals conformational changes upon activation and the molecular basis for G-protein selectivity.