University of Sussex

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The crystal structure of human eukaryotic release factor eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis

journal contribution
posted on 2023-06-10, 04:07 authored by Haiwei Song, Piere Mugnier, Amit K Das, Helen WebbHelen Webb, David R Evans, Mick F Tuite, Brian A Hemmings, David Barford
The release factor eRF1 terminates protein biosynthesis by recognizing stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase center. The crystal structure of human eRF1 to 2.8 Å resolution, combined with mutagenesis analyses of the universal GGQ motif, reveals the molecular mechanism of release factor activity. The overall shape and dimensions of eRF1 resemble a tRNA-molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stern of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase center. A conserved groove on domain 1, 80 Å from the GGQ motif, is proposed to form the codon recognition site.


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Elsevier BV



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United States

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  • Biochemistry Publications

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