Structural modelling of the complex of leucyl-tRNA synthetase and mis-aminoacylated tRNALeu.
To assure fidelity of translation, class Ia aminoacyl-tRNA synthetases (aaRSs) edit mis-aminoacylated tRNAs. Mis-attached amino acids and structural water molecules are not included simultaneously in the current crystal structures of the aaRSctRNA complexes, where the 3'-ends (adenine 76; A76) are bound to the editing sites. A structural model of the completely solvated leucyl-tRNA synthetase complexed with valyl-tRNALeu was constructed by exploiting molecular dynamics simulations modified for the present modelling. The results showed that the ribose conformation of A76 is distinct from those observed in the above-mentioned crystal structures, which could be derived from structural constraints in a sandwiched manner induced by the mis-attached valine and tRNALeu.
Hagiwara
Yohsuke
Y
Center for Computational Sciences, University of Tsukuba, Division of Materials and Life Sciences, Tennodai 1-1-1, Tsukuba, Ibaraki 305-8571, Japan; Graduate School of Pure and Applied Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba Science City, Ibaraki 305-8571, Japan.
Nureki
Osamu
O
Tateno
Masaru
M
D049148:Aminoacylation; D001665:Binding Sites; D018360:Crystallography, X-Ray; D007935:Leucine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D017434:Protein Structure, Tertiary; D012356:RNA, Transfer, Leu / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity; D016963:Thermus thermophilus / Q000201:enzymology; D014633:Valine / Q000378:metabolism
D012356:RNA, Transfer, Leu; D007935:Leucine-tRNA Ligase; D014633:Valine