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. 2000 Sep;79(3):1670–1678. doi: 10.1016/S0006-3495(00)76416-2

Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures.

W Wriggers 1, R K Agrawal 1, D L Drew 1, A McCammon 1, J Frank 1
PMCID: PMC1301058  PMID: 10969026

Abstract

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 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.

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Selected References

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