1y2q
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span> |
|GENE= thrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi]) | |GENE= thrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1y2r|1Y2R]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y2q OCA], [http://www.ebi.ac.uk/pdbsum/1y2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y2q RCSB]</span> | ||
}} | }} | ||
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[[Category: trna-synthetase]] | [[Category: trna-synthetase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:58:04 2008'' |
Revision as of 21:58, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | thrS (Pyrococcus abyssi) | ||||||
| Activity: | Threonine--tRNA ligase, with EC number 6.1.1.3 | ||||||
| Related: | 1Y2R
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi
Overview
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.
About this Structure
1Y2Q is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
Reference
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
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