Binding and enantiomeric selectivity of threonyl-tRNA synthetase

J Am Chem Soc. 2009 Mar 25;131(11):3848-9. doi: 10.1021/ja9002124.

Abstract

A combination of MD simulations and free energy calculations have been used to propose a new model for the binding of amino acids to threonyl-tRNA-synthetase which not only yields a stable binding mode for l-Ser but also can explain the mechanism by which the editing domains of aminoacyl-tRNA-synthetases are enantiomeric selective preferentially binding d-amino acids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry
  • Amino Acids / metabolism
  • Computer Simulation
  • Models, Molecular
  • Protein Binding
  • Serine / chemistry
  • Serine / metabolism
  • Stereoisomerism
  • Thermodynamics
  • Threonine-tRNA Ligase / chemistry*
  • Threonine-tRNA Ligase / metabolism

Substances

  • Amino Acids
  • Serine
  • Threonine-tRNA Ligase