The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known (PUBMED:10676813). 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 centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site (PUBMED:10676813). This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.
This domain is found in the release factor eRF1 which terminates protein biosynthesis by recognizing stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known [ (PUBMED:10676813) ]. 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 centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site [ (PUBMED:10676813) ].
This domain is also found in other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.
Family alignment:
There are 5259 eRF1_1 domains in 5257 proteins in SMART's nrdb database.
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Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing eRF1_1 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with eRF1_1 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing eRF1_1 domain in the selected taxonomic class.
The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis.
Cell. 2000; 100: 311-21
Display abstract
The release factor eRF1 terminates protein biosynthesis by recognizing stopcodons at the A site of the ribosome and stimulating peptidyl-tRNA bondhydrolysis at the peptidyl transferase center. The crystal structure of humaneRF1 to 2.8 A resolution, combined with mutagenesis analyses of the universal GGQmotif, reveals the molecular mechanism of release factor activity. The overallshape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 ofeRF1 corresponding to the anticodon loop, aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at anexposed tip of domain 2 suggests that the Gln residue coordinates a watermolecule to mediate the hydrolytic activity at the peptidyl transferase center. Aconserved groove on domain 1, 80 A from the GGQ motif, is proposed to form thecodon recognition site.
