Insights into translational termination from the structure of RF2 bound to the ribosome

Albert Weixlbaumer, Hong Jin, Cajetan Neubauer, Rebecca M. Voorhees, Sabine Petry, Ann C. Kelley, Venki Ramakrishnan

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209 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)953-956
Number of pages4
JournalScience
Volume322
Issue number5903
DOIs
StatePublished - Nov 7 2008

All Science Journal Classification (ASJC) codes

  • General

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    Weixlbaumer, A., Jin, H., Neubauer, C., Voorhees, R. M., Petry, S., Kelley, A. C., & Ramakrishnan, V. (2008). Insights into translational termination from the structure of RF2 bound to the ribosome. Science, 322(5903), 953-956. https://doi.org/10.1126/science.1164840