Two interpretations of similar structures for the same molecular machine illustrate the limits of inferring biochemical mechanism from protein structure.

Understanding of bacterial protein degradation is illuminated by cryo-EM structures of the substrate-bound ClpXP complex from Neisseria meningitidis at 2.3 to 3.3 Å resolution.

Cryo-EM structures of the ClpXP protease reveal how protein substrates are bound, show how spiral ClpX hexamers bind symmetry-mismatched heptameric ClpP rings, and suggest mechanisms for processive substrate translocation.

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.

A naturally-occurring small molecule acts as a chemical chaperone in vivo to alter the folding of a budding yeast septin and promote an oligomerization pathway that was lost during evolution.

GTP binding induces rearrangement of S-OPA1 assembly on membrane and thus triggers membrane remodeling with reduced curvature.

Glutamatergic projections from basolateral to central amygdala, implicated in neuropsychiatric disorders, develop rapidly during early postnatal period and their development is modulated via endogenously active kainate receptors.

A single gene allele underlies differences in aneuploidy tolerance in yeast.

Two genetically distinct Stxbp1 haploinsufficiency mouse models exhibit seizures and impairments in cognitive, psychiatric, and motor functions, representing robust preclinical models of STXBP1 encephalopathy with both construct and face validity.