W. Wriggers et al., Domain motions of EF-G bound to the 70S ribosome: Insights from a hand-shaking between multi-resolution structures, BIOPHYS J, 79(3), 2000, pp. 1670-1678
Molecular modeling and information processing techniques were combined to r
efine the structure of translocase (EF-G) in the ribosome-bound form agains
t data from cryoelectron microscopy (cryo-EM). We devised a novel multi-sca
le refinement method based on vector quantization and force-field methods t
hat gives excellent agreement between the flexibly docked structure of GDP
. EF-G and the cryo-EM density map at 17 Angstrom resolution. The refinemen
t reveals a dramatic "induced fit" conformational change on the 70S ribosom
e, mainly involving EF-G's domains III, IV, and V. The rearrangement of EF-
G's structurally preserved regions, mediated and guided by flexible linkers
, defines the site of interaction with the GTPase-associated center of the
ribosome.