Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
A D-amino acid editing module coupled to the translational apparatus in archaea.,Dwivedi S, Kruparani SP, Sankaranarayanan R Nat Struct Mol Biol. 2005 Jun;12(6):556-7. Epub 2005 May 22. PMID:15908961[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dwivedi S, Kruparani SP, Sankaranarayanan R. A D-amino acid editing module coupled to the translational apparatus in archaea. Nat Struct Mol Biol. 2005 Jun;12(6):556-7. Epub 2005 May 22. PMID:15908961 doi:http://dx.doi.org/10.1038/nsmb943
