Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hagiwara Y,Nureki O,Tateno Mdoi
10.1016/j.febslet.2009.01.049subject
Has Abstractpub_date
2009-02-18 00:00:00pages
825-30issue
4eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00083-0journal_volume
583pub_type
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