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Biophys J, September 2000, p. 1670-1678, Vol. 79, No. 3

Domain Motions of EF-G Bound to the 70S Ribosome: Insights from a Hand-Shaking between Multi-Resolution Structures

Willy Wriggers,*dagger Rajendra K. Agrawal,Dagger § Devin Lee Drew,* Andrew McCammon,* and Joachim FrankDagger

 *Department of Chemistry and Biochemistry, and Department of Pharmacology, University of California, San Diego, La Jolla, California 92093-0365;  dagger Departments of Cell Biology and Molecular Biology, The Scripps Research Institute, La Jolla, California 92037;  Dagger Department of Biomedical Sciences, State University of New York at Albany, Empire State Plaza, Albany, New York 12201-0509; and  Howard Hughes Medical Institute, Health Research, Inc. at the  §Wadsworth Center, Empire State Plaza, Albany, New York 12201-0509 USA

Molecular modeling and information processing techniques were combined to refine the structure of translocase (EF-G) in the ribosome-bound form against data from cryoelectron 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 Å 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.

Biophys J, September 2000, p. 1670-1678, Vol. 79, No. 3
© 2000 by the Biophysical Society   0006-3495/00/09/1670/09  $2.00


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