ArticleBiophysical journal2000
Domain motions of EF-G bound to the 70S ribosome: insights from a hand-shaking between multi-resolution structures.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 85 citations in OpenAlex.
- EF-G Mutations Reveal Correlation between Power Stroke and Translocation Fidelity in Protein Synthesis.bioRxiv : the preprint server for biology · 2025Article
- Refinement of AlphaFold2 Models against Experimental Cryo-EM Density Maps at 4-6Å Resolution.Proceedings. IEEE International Conference on Bioinformatics and Biomedicine · 2022Article
- Refinement of AlphaFold2 models against experimental and hybrid cryo-EM density maps.QRB discovery · 2022Article
- A Tool for Segmentation of Secondary Structures in 3D Cryo-EM Density Map Components Using Deep Convolutional Neural Networks.Frontiers in bioinformatics · 2021Article
- Cylindrical Similarity Measurement for Helices in Medium-Resolution Cryo-Electron Microscopy Density Maps.Journal of chemical information and modeling · 2020Article
- Analytical Approaches to Improve Accuracy in Solving the Protein Topology Problem.Molecules (Basel, Switzerland) · 2018Article
- Quantitative Characterization of Domain Motions in Molecular Machines.The journal of physical chemistry. B · 2017Article
- Ribosome Mechanics Informs about Mechanism.Journal of molecular biology · 2016Review
- Numerical geometry of map and model assessment.Journal of structural biology · 2015Article
- Functional Importance of Mobile Ribosomal Proteins.BioMed research international · 2015Review
- GTP hydrolysis by EF-G synchronizes tRNA movement on small and large ribosomal subunits.The EMBO journal · 2014Article
- A conserved proline switch on the ribosome facilitates the recruitment and binding of trGTPases.Nature structural & molecular biology · 2012Article
- Outcome of the first electron microscopy validation task force meeting.Structure (London, England : 1993) · 2012Article
- Evolutionary bidirectional expansion for the tracing of alpha helices in cryo-electron microscopy reconstructions.Journal of structural biology · 2012Article
- Brownian dynamics study of the association between the 70S ribosome and elongation factor G.Biopolymers · 2011Article
- Molecular dynamics of EF-G during translocation.Proteins · 2011Article
- Molecular dynamics of ribosomal elongation factors G and Tu.European biophysics journal : EBJ · 2011Article
- Evolutionary tabu search strategies for the simultaneous registration of multiple atomic structures in cryo-EM reconstructions.Journal of structural biology · 2010Article
- Structure and dynamics of a processive Brownian motor: the translating ribosome.Annual review of biochemistry · 2010Review
- Molecular dynamics flexible fitting: a practical guide to combine cryo-electron microscopy and X-ray crystallography.Methods (San Diego, Calif.) · 2009Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.