1y2q | pdb_00001y2q
From Proteopedia
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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 AlsoReferences
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