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

Article Details

Citation

Weixlbaumer A, Jin H, Neubauer C, Voorhees RM, Petry S, Kelley AC, Ramakrishnan V

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

Science. 2008 Nov 7;322(5903):953-6. doi: 10.1126/science.1164840.

PubMed ID
18988853 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
30S ribosomal protein S14 type ZP0DOY6Details
30S ribosomal protein S17P0DOY7Details
30S ribosomal protein S8P0DOY9Details