1DT9

THE CRYSTAL STRUCTURE OF HUMAN EUKARYOTIC RELEASE FACTOR ERF1-MECHANISM OF STOP CODON RECOGNITION AND PEPTIDYL-TRNA HYDROLYSIS

Summary for 1DT9

• Entry DOI: 10.2210/pdb1dt9/pdb
• Descriptor: PROTEIN (EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1) (2 entities in total)
• Functional Keywords: erf1, trna mimicry, protein sythesis, stop codon recognition, peptidyl-trna hydrolysis, translation
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 49092.74

Authors

Frolova, L. (deposition date: 2000-01-12, release date: 2000-02-02, Last modification date: 2024-02-07)

Primary citation

Song, H.,Mugnier, P.,Das, A.K.,Webb, H.M.,Evans, D.R.,Tuite, M.F.,Hemmings, B.A.,Barford, D.
The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis.
Cell(Cambridge,Mass.), 100:311-321, 2000

PubMed 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.

PubMed: 10676813
DOI: 10.1016/S0092-8674(00)80667-4

Experimental method

X-RAY DIFFRACTION (2.7 Å)