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Brief Communication
Nature Structural & Molecular Biology  12, 556 - 557 (2005)
Published online: 22 May 2005; | doi:10.1038/nsmb943

A D-amino acid editing module coupled to the translational apparatus in archaea

Shweta Dwivedi, Shobha P Kruparani & Rajan Sankaranarayanan

Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.

Correspondence should be addressed to Rajan Sankaranarayanan sankar@ccmb.res.in
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.


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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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