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1y2q
From Proteopedia
| 1y2q, resolution 1.95Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Gene: | thrS (Pyrococcus abyssi) | ||||||||
| Activity: | Threonine--tRNA ligase, with EC number 6.1.1.3 | ||||||||
| Related: | 1y2r | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1y2q is a 1 chain structure with sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
See Also
Reference
- 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:10.1038/nsmb943
- Dwivedi S, Kruparani SP, Sankaranarayanan R. Cloning, expression, purification, crystallization and preliminary X-ray crystallographic investigations of a unique editing domain from archaebacteria. Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1662-4. Epub 2004, Aug 26. PMID:15333948 doi:10.1107/S0907444904017329
