Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation
- C. Spahn, Maria G. Gomez-Lorenzo, J. Frank
- Biology, ChemistryEMBO Journal
- 10 March 2004
An 11.7‐Å‐resolution cryo‐EM map of the yeast 80S·eEF2 complex in the presence of the antibiotic sordarin was interpreted in molecular terms, revealing large conformational changes within eEF2 and…
Structural Basis for Gating and Activation of RyR1
- A. D. Georges, O. Clarke, J. Frank
- 22 September 2016
Structure of the signal recognition particle interacting with the elongation-arrested ribosome
- M. Halić, T. Becker, R. Beckmann
- Biology, Computer ScienceNature
- 26 February 2004
The model shows how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation-factor-binding site of the ribosome, explaining its elongation arrest activity.
Hepatitis C Virus IRES RNA-Induced Changes in the Conformation of the 40S Ribosomal Subunit
- C. Spahn, J. Kieft, Joachim Frank
- 9 March 2001
A cryo-electron microscopy map of the hepatitis C virus IRES bound to the 40S ribosomal subunit at about 20 Å resolution is presented, suggesting a mechanism for IRES-mediated positioning of mRNA in the Ribosomal decoding center.
Structure of the Mammalian Ribosomal 43S Preinitiation Complex Bound to the Scanning Factor DHX29
- Y. Hashem, A. D. Georges, J. Frank
- Biology, ChemistryCell
- 23 May 2013
Cryo-EM Visualization of a Viral Internal Ribosome Entry Site Bound to Human Ribosomes The IRES Functions as an RNA-Based Translation Factor
- C. Spahn, E. Jan, Anke M. Mulder, R. Grassucci, P. Sarnow, J. Frank
- Biology, Computer ScienceCell
- 20 August 2004
The ribosome at improved resolution: new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles.
- P. Penczek, R. Grassucci, J. Frank
- 1 March 1994
Solution Structure of the E. coli 70S Ribosome at 11.5 Å Resolution
- I. Gabashvili, R. Agrawal, P. Penczek
- 3 March 2000
Structure of a mammalian ryanodine receptor
The closed-state structure of the 2.3-megadalton complex of the rabbit skeletal muscle type 1 RyR (RyR1), solved by single-particle electron cryomicroscopy at an overall resolution of 4.8 Å is reported.
Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation.
- R. Agrawal, P. Penczek, R. Grassucci, J. Frank
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 26 May 1998
Three-dimensional cryo-electron microscopy has visualized elongation factor G in a ribosome-EF-G-GDP-fusidic acid complex, revealing a large conformational change mainly associated with domain IV, the domain that mimics the shape of the anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog.