Extended Data Fig. 7: Effect of sordarin binding to eEF2 in the context of eukaryotic translocation.

a-c, Global alignments reflecting general conservation of overall eEF2 conformation during early, in a, and late states of translocation, in b and c. d-f, Domain III alignment shows displacement of eEF2 domain V towards the interface with domain III. g-I, Zoom on the sordardin binding site for respective structural superimpositions on eEF2 domain III, as shown in d-f. The arrow indicates the displacement of domain V relative to domain III. Remodelling of the switch loop 2 (sw2) has not been observed. Structural alignments are performed for late translocation states before, in b, e and h, and after GTP hydrolysis, in c, f and i. eEF2 domains are colored as follows: domain I in green, domain II in magenta, domain III in pink, domain IV in red, and domain V in blue. Unfiltered, unsharpened of sordarin is shown at σ = 4 and depicted in orange. Lighter nuances correspond to structures without sordardin, TI-1* and TI-4*. j, Chemical structure of sordarin.