Willy Wriggers, Rajendra K. Agrawal, Devin Lee Drew, J. Andrew McCammon, and Joachim Frank. Domain Movements of EF-G bound to the 70S Ribosome: Insights from a Hand-Shaking between Multi-Resolution Structures. Biophysical Journal, Vol. 79, pp. 1670-1678.
Molecular modeling and information processing techniques were combined to refine the structure of translocase (EF-G) in the ribosome-bound form against data from cryo-electron microscopy (cryo-EM). We devised a novel multi-scale refinement method based on vector quantization and force-field methods that gives excellent agreement between the flexibly docked structure of GDP.EF-G and the cryo-EM density map at 17 A resolution. The refinement reveals a dramatic ``induced fit'' conformational change on the 70S ribosome, 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.
