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

Citation
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
Citations number
49
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOPHYSICAL JOURNAL
ISSN journal
00063495 → ACNP
Volume
79
Issue
3
Year of publication
2000
Pages
1670 - 1678
Database
ISI
SICI code
0006-3495(200009)79:3<1670:DMOEBT>2.0.ZU;2-K
Abstract
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.