1Y2Q

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi

Summary for 1Y2Q

Entry DOI	10.2210/pdb1y2q/pdb
Related	1Y2R
Descriptor	Threonyl-tRNA synthetase (2 entities in total)
Functional Keywords	beta-alpha-beta fold, editing domain, trna-synthetase, ligase
Biological source	Pyrococcus abyssi
Cellular location	Cytoplasm: Q9UZ14
Total number of polymer chains	1
Total formula weight	16281.80
Authors	Dwivedi, S.,Kruparani, S.P.,Sankaranarayanan, R. (deposition date: 2004-11-23, release date: 2005-06-14, Last modification date: 2024-03-13)
Primary citation	Dwivedi, S.,Kruparani, S.P.,Sankaranarayanan, R. A D-amino acid editing module coupled to the translational apparatus in archaea Nat.Struct.Mol.Biol., 12:556-557, 2005 Cited by PubMed Abstract: 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. PubMed: 15908961 DOI: 10.1038/nsmb943 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation