Model of the structure of the eukaryotic ribosomal translation termination complex

作者：Vorobjev Yu N^*; Kisselev L L

来源：Molecular Biology, 2007, 41(1): 93-101.

DOI：10.1134/S002689330701013X

• molecular modeling
• eukaryotes
• class 1 release factor
• eRF1
• ribosomal translation termination complex
• conformational rearrangements

Models of the atomic structure of the eukaryotic translation termination complex containing mRNA, P-site tRNA(Phe), human class 1 release factor eRF1, and 80S ribosome, were constructed by computational modeling. The modeling was based on the assumed structural-functional similarity between the tRNA and eFR1 molecules in the ribosomal A site. The known atomic structure of the 70S ribosome complexed with mRNA as well as the P-and A-site tRNAs(Phe) was used as a structural template for the modeling. The eRF1 molecule bound in the A site undergoes substantial conformational changes so that the mutual configuration of the N and M domains matches the overall tRNA shape. Two models of eRF1 binding to mRNA at the A site in the presence of P-site tRNA(Phe) were generated. A characteristic of these models is complementary interactions between the mRNA stop codon and the grooves at different sides of the surface of the eRF1 fragment, containing helix alpha 2, NIKS loop, and helix alpha 3 of the N domain. In model 1, the nucleotides of the mRNA stop codon at the A site are approximately equidistant (similar to 15 angstrom) from the N (motifs NIKS and YxCxxxF) and C domains. In model 2, the stop codon is close to the N-domain motifs NIKS and YxCxxxF. Both models fit genetic and biochemical experimental data. The choice of a particular model requires additional studies.

• 出版日期2007-2