Interaction of tyrosyl aryl dipeptides with S. aureus tyrosyl tRNA synthetase: inhibition and crystal structure of a complex

Bioorg Med Chem Lett. 1999 Oct 4;9(19):2859-62. doi: 10.1016/s0960-894x(99)00488-6.

Abstract

Tyrosyl aryl dipeptide inhibitors of S. aureus tyrosyl tRNA synthetase have been identified with IC50 values down to 0.5 microM. A crystal structure of the enzyme complexed to one of the inhibitors shows occupancy of the tyrosyl binding pocket coupled with inhibitor interactions to key catalytic residues.

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray
  • Dipeptides / chemistry*
  • Dipeptides / pharmacology
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology
  • Glycine / analogs & derivatives
  • Models, Molecular
  • Molecular Structure
  • Protein Binding
  • Staphylococcus aureus / enzymology*
  • Tyrosine / analogs & derivatives
  • Tyrosine-tRNA Ligase / antagonists & inhibitors
  • Tyrosine-tRNA Ligase / chemistry*

Substances

  • Dipeptides
  • Enzyme Inhibitors
  • Tyrosine
  • Tyrosine-tRNA Ligase
  • Glycine