Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
- 14 April 2003
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature Structural & Molecular Biology
- Vol. 10 (5), 379-385
- https://doi.org/10.1038/nsb923
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Coupling of GTP Hydrolysis by Elongation Factor G to Translocation and Factor Recycling on the RibosomeBiochemistry, 2002
- Translocation of tRNA during protein synthesisFEBS Letters, 2002
- Ribosome Structure and the Mechanism of TranslationCell, 2002
- Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome.Nature Structural & Molecular Biology, 2000
- Three-dimensional cryo-electron microscopy localization of EF2 in the Saccharomyces cerevisiae 80S ribosome at 17.5 A resolutionThe EMBO Journal, 2000
- Large-Scale Movement of Elongation Factor G and Extensive Conformational Change of the Ribosome during TranslocationCell, 2000
- Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocationProceedings of the National Academy of Sciences of the United States of America, 1998
- The Conformational Properties of Elongation Factor G and the Mechanism of TranslocationBiochemistry, 1997
- Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosomeNature, 1997
- Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP AnalogScience, 1995