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Structure paper

TitlePost-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea
Journal, issue, pagesEmbo J., Vol. 25, Page 4152-4162, Year 2006
Publish dateJul 6, 2006 (structure data deposition date)
AuthorsHussain, T. / Kruparani, S.P. / Pal, B. / Dock-Bregeon, A.C. / Dwivedi, S. / Shekar, M.R. / Sureshbabu, K. / Sankaranarayanan, R.
External linksEmbo J. / PubMed:16902403
MethodsX-ray diffraction
Resolution1.86 - 2.6 Å
Structure data

PDB-2hkz:
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with L-serine
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2hl0:
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-2hl1:
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with seryl-3'-aminoadenosine
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-2hl2:
Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-SER:
SERINE

ChemComp-HOH:
WATER

ChemComp-A3S:
SERINE-3'-AMINOADENOSINE

ChemComp-SSA:
5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE

Source
  • pyrococcus abyssi (archaea)
KeywordsLIGASE / translation / editing / aminoacyl-tRNA synthetase / enzyme mechanism / enantioselectivity

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