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TitleTwo complementary enzymes for threonylation of tRNA in crenarchaeota: crystal structure of Aeropyrum pernix threonyl-tRNA synthetase lacking a cis-editing domain
Journal, issue, pagesJ. Mol. Biol., Vol. 394, Page 286-296, Year 2009
Publish dateJun 7, 2009 (structure data deposition date)
AuthorsShimizu, S. / Juan, E.C.M. / Sato, Y. / Miyashita, Y. / Hoque, M.M. / Suzuki, K. / Sagara, T. / Tsunoda, M. / Sekiguchi, T. / Dock-Bregeon, A.-C. ...Shimizu, S. / Juan, E.C.M. / Sato, Y. / Miyashita, Y. / Hoque, M.M. / Suzuki, K. / Sagara, T. / Tsunoda, M. / Sekiguchi, T. / Dock-Bregeon, A.-C. / Moras, D. / Takenaka, A.
External linksJ. Mol. Biol. / PubMed:19761773
MethodsX-ray diffraction
Resolution2.3 - 2.5 Å
Structure data

PDB-3a31:
Crystal structure of putative threonyl-tRNA synthetase ThrRS-1 from Aeropyrum pernix (selenomethionine derivative)
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3a32:
Crystal structure of putative threonyl-tRNA synthetase ThrRS-1 from Aeropyrum pernix
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • aeropyrum pernix (archaea)
KeywordsLIGASE / threonyl-tRNA synthetase / Aeropyrum pernix K1 / protein biosynthesis / Aminoacyl-tRNA synthetase / ATP-binding / Metal-binding / Nucleotide-binding

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