Browse our latest Structural Biology and Molecular Biophysics articles

La-related protein 1 specifically and directly binds the 5' cap and first nucleotide of mRNAs encoding ribosomal proteins and translation factors, inhibiting the assembly of translation initiation factors on these messages and therefore their translation.

The resurrection of ancient ancestral intrinsically disordered proteins reveals the evolution of a protein-protein interaction in molecular detail.

The canonical model that the bacterial replisome tightly holds on to its polymerases is challenged by the visualization of rapid holoenzyme exchange, both in vitro and in vivo.

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.

A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.

Fam20A, a pseudokinase involved in the formation of tooth enamel, binds ATP in an unexpected orientation.

Along with preventing D-amino acids from being incorporated into proteins, D-aminoacyl-tRNA deacylase clears achiral glycine that is incorrectly attached to tRNA^Ala.

Extensive molecular dynamics simulations enhanced by advanced sampling techniques give a detailed view of p38α canonical activation mechanism, which reveals novel key electrostatic interactions that are put in context of existing experimental data.

A few SNARE complexes suffice to fuse membranes, but many more are needed to dilate the nascent fusion pore by molecular crowding for efficient neurotransmitter or hormone release during exocytosis.

After DNA replication, nucleosomes are assembled by two histone chaperone complexes each bound to an H3-H4 histone dimer, suggesting the feasibility for a semi-conservative mode of epigenome inheritance.