| Literature DB >> 10676813 |
H Song1, P Mugnier, A K Das, H M Webb, D R Evans, M F Tuite, B A Hemmings, D Barford.
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 A 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 stem 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 A from the GGQ motif, is proposed to form the codon recognition site.Entities:
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Year: 2000 PMID： 10676813 DOI： 10.1016/s0092-8674(00)80667-4
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582