Song, Haiwei and Mugnier, Pierre M. and Das, Amit K. and Webb, Helen M. and Evans, David R. and Tuite, Mick F. and 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 (3). pp. 311-321. ISSN 0092-8674. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
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 Angstrom 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 Gin residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase center. A conserved groove on domain 1, 80 Angstrom from the GGQ motif, is proposed to form the codon recognition site.
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||A. Xie|
|Date Deposited:||21 Jun 2009 19:28|
|Last Modified:||10 Jun 2014 12:41|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/16654 (The current URI for this page, for reference purposes)|