Published November 7, 2008
| Accepted Version + Supplemental Material
Journal Article
Open
Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome
Chicago
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Abstract
The termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor (RF), which then catalyzes the hydrolysis of the nascent protein chain from the P-site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release.
Additional Information
© 2010 American Association for the Advancement of Science. 19 August 2008; accepted 26 September 2008. We thank M. Schmeing for his useful comments and M. Fuchs and C. Schulze-Briese for their help and advice with data collection at the Swiss Light Source. This work was supported by MRC UK, a program grant from the Wellcome Trust, and awards from the Agouron Institute and Louis-Jeantet Foundation. C.N. is supported by a Boehringer-Ingelheim fellowship and R.M.V. is supported by a Gates-Cambridge fellowship. Coordinates for the structure have been deposited in the Protein Data Bank with accession codes 2jl5 to 2jl8. V.R. holds stock options in Rib-X Pharmaceuticals, a company that develops antibacterial drugs that target the ribosome.Attached Files
Accepted Version - ukmss-3707.pdf
Supplemental Material - Weixlbaumer-SOM.pdf
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Weixlbaumer-SOM.pdf
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Additional details
- PMCID
- PMC2642913
- Eprint ID
- 84353
- Resolver ID
- CaltechAUTHORS:20180117-080027343
- Medical Research Council (UK)
- Wellcome Trust
- Agouron Institute
- Louis-Jeantet Foundation
- Boehringer-Ingelheim
- Gates-Cambridge Scholarship
- Created
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2018-01-17Created from EPrint's datestamp field
- Updated
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2023-02-28Created from EPrint's last_modified field