A D-amino acid editing module coupled to the translational apparatus in archaea.
We report the crystal structure of an archaea-specific editing domain of threonyl-tRNA synthetase that reveals a marked structural similarity to D-amino acid deacylases found in eubacteria and eukaryotes. The domain can bind D-amino acids despite a low sequence identity to other D-amino acid deacylases. These results together indicate the presence of these deacylases in all three kingdoms of life. This underlines an important role they may have played in enforcing homochirality during translation.
Dwivedi
Shweta
S
Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.
Kruparani
Shobha P
SP
Sankaranarayanan
Rajan
R
D000596:Amino Acids; D001105:Archaea / Q000235:genetics*; D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods; D014176:Protein Biosynthesis; D017393:RNA Editing; D013237:Stereoisomerism; D013914:Threonine-tRNA Ligase / Q000235:genetics
D000596:Amino Acids; D013914:Threonine-tRNA Ligase