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Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation
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 andExpand
Structure of the signal recognition particle interacting with the elongation-arrested ribosome
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. Expand
Structure of the Mammalian Ribosomal 43S Preinitiation Complex Bound to the Scanning Factor DHX29
The structure of the mammalian DHX29-bound 43S complex is presented and it is revealed that eIF2 interacts with the 40S subunit via its α subunit and supports Met-tRNAi(Met) in an unexpected P/I orientation (eP/I). Expand
Hepatitis C Virus IRES RNA-Induced Changes in the Conformation of the 40S Ribosomal Subunit
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. Expand
Cryo-EM Visualization of a Viral Internal Ribosome Entry Site Bound to Human Ribosomes The IRES Functions as an RNA-Based Translation Factor
Cryo-EM structures of the CrPV IRES bound to the human ribosomal 40S subunit and to the 80S ribosome show that CrPVs-like IRES elements seem to act as RNA-based translation factors. Expand
Solution Structure of the E. coli 70S Ribosome at 11.5 Å Resolution
Comparison of double-stranded RNA regions and positions of proteins identified in both cryo-EM and X-ray maps indicates good overall agreement but points to rearrangements of ribosomal components required for the subunit association. Expand
The ribosome at improved resolution: new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles.
New methods of data collection and image processing are developed and applied to the 70S Escherichia coli ribosome and a method of orientation search is proposed, which makes it possible to relate random-conical data sets to one another even if they are collected from low-tilt micrographs. Expand
Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex.
Cryo-electron microscopy of the ribosome-Sec61 complex and a three-dimensional reconstruction showed that the Sec61 oligomer is attached to the large ribosomal subunit by a single connection, strongly suggesting that both structures function together in the translocation of proteins across the endoplasmic reticulum membrane. Expand
Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation.
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. Expand
Structural Basis for Gating and Activation of RyR1
Cryo-EM reconstructions of RyR1 in multiple functional states reveal the structural basis of channel gating and ligand-dependent activation, enabling analyses of conformational changes associated with gating. Expand