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

Song, Haiwei, Mugnier, Piere, Das, Amit K, Webb (Biochemistry), Helen M, Evans, David R, Tuite, Mick F, Hemmings, Brian A and Barford, David (2000) The crystal structure of human eukaryotic release factor eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell, 100. pp. 311-321. ISSN 0092-8674

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Abstract

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.

Item Type: Article
Keywords: Amino Acid Sequence;Codon, Terminator;Crystallography;Humans;Hydrolysis;Models, Molecular;Molecular Mimicry;Molecular Sequence Data;Peptide Chain Termination, Translational;Peptide Termination Factors;RNA, Transfer;RNA, Transfer, Amino Acyl;Recombinant Proteins;Sequence Homology, Amino Acid
Schools and Departments: School of Life Sciences > Biochemistry
SWORD Depositor: Mx Elements Account
Depositing User: Mx Elements Account
Date Deposited: 01 Jul 2022 08:04
Last Modified: 01 Jul 2022 08:15
URI: http://sro.sussex.ac.uk/id/eprint/106692

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