Structure of the Escherichia coli ribosomal termination complex with release factor 2
- 1 January 2003
- journal article
- Published by Springer Nature in Nature
- Vol. 421 (6918) , 90-94
- https://doi.org/10.1038/nature01225
Abstract
Nature is the international weekly journal of science: a magazine style journal that publishes full-length research papers in all disciplines of science, as well as News and Views, reviews, news, features, commentaries, web focuses and more, covering all branches of science and how science impacts upon all aspects of society and life.Keywords
This publication has 28 references indexed in Scilit:
- Release of Peptide Promoted by the GGQ Motif of Class 1 Release Factors Regulates the GTPase Activity of RF3Molecular Cell, 2002
- Bacterial Polypeptide Release Factor RF2 Is Structurally Distinct from Eukaryotic eRF1Molecular Cell, 2001
- A Posttermination Ribosomal Complex Is the Guanine Nucleotide Exchange Factor for Peptide Release Factor RF3Cell, 2001
- Crystal Structure of the Ribosome at 5.5 Å ResolutionScience, 2001
- Translational termination comes of ageTrends in Biochemical Sciences, 2000
- Single-particle electron cryo-microscopy: towards atomic resolutionQuarterly Reviews of Biophysics, 2000
- The Crystal Structure of Human Eukaryotic Release Factor eRF1—Mechanism of Stop Codon Recognition and Peptidyl-tRNA HydrolysisCell, 2000
- A tripeptide ‘anticodon’ deciphers stop codons in messenger RNANature, 2000
- Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysisRNA, 1999
- Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent mannerThe EMBO Journal, 1997