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Structure paper

TitleTwo crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate
Journal, issue, pagesJ. Biochem., Vol. 145, Page 555-563, Year 2009
Publish dateAug 22, 2008 (structure data deposition date)
AuthorsSakurama, H. / Takita, T. / Mikami, B. / Itoh, T. / Yasukawa, K. / Inouye, K.
External linksJ. Biochem. / PubMed:19174549
MethodsX-ray diffraction
Resolution2.1 - 2.2 Å
Structure data

PDB-3e9h:
Lysyl-tRNA synthetase from Bacillus stearothermophilus complexed with L-Lysylsulfamoyl adenosine
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3e9i:
Lysyl-tRNA synthetase from Bacillus stearothermophilus complexed with L-Lysine hydroxamate-AMP
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-KAA:
5'-O-[(L-LYSYLAMINO)SULFONYL]ADENOSINE

ChemComp-HOH:
WATER

ChemComp-XAH:
5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

Source
  • bacillus stearothermophilus (bacteria)
KeywordsLIGASE / aminoacyl tRNA synthetase / PROTEIN BIOSYNTHESIS / Aminoacyl-tRNA synthetase / ATP-binding / Cytoplasm / Magnesium / Metal-binding / Nucleotide-binding

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