Paola Fucini

TL;DR: Cryoelectron microscopy analysis is used to resolve two previously unseen subpopulations within Thermus thermophilus EF-G–ribosome complexes at subnanometre resolution and provides direct structural and mechanistic insight into the ‘missing link’ in terms of tRNA intermediates involved in the universally conserved translocation process.

TL;DR: The results suggest that L11 acts as a molecular switch to control L7 binding and plays a pivotal role in positioning one L7-CTD monomer on the G' subdomain ofEF-G to regulate EF-G turnover during protein synthesis.

TL;DR: The crystal structure of the oxazolidinone linezolid bound to the Deinococcus radiodurans 50S ribosomal subunit is determined and a model whereby oxazolicinones impart their inhibitory effect by perturbing the correct positioning of tRNAs on the ribosome is presented.

TL;DR: The results show that emerging mass spectrometric techniques can be used to characterize a fully functional biological assembly as well as its isolated components.

TL;DR: The results show that tiamulin is located within the peptidyl transferase center (PTC) of the 50S ribosomal subunit with its tricyclic mutilin core positioned in a tight pocket at the A‐tRNA binding site, thus explaining the molecular mechanism of the antimicrobial activity of the pleuromutilin class of antibiotics.