Structural modelling of the complex of leucyl-tRNA synthetase and mis-aminoacylated tRNALeu.

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 Lett

journal_title

FEBS letters

authors

Hagiwara Y,Nureki O,Tateno M

doi

10.1016/j.febslet.2009.01.049

subject

Has Abstract

pub_date

2009-02-18 00:00:00

pages

825-30

issue

4

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00083-0

journal_volume

583

pub_type

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