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Structure paper

TitleCatalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic states
Journal, issue, pagesNucleic Acids Res., Vol. 36, Page 1288-1299, Year 2008
Publish dateAug 5, 2007 (structure data deposition date)
AuthorsShen, N. / Zhou, M. / Yang, B. / Yu, Y. / Dong, X. / Ding, J.
External linksNucleic Acids Res. / PubMed:18180246
MethodsX-ray diffraction
Resolution2.4 - 2.8 Å
Structure data

PDB-2quh:
Crystal structures of human tryptophanyl-tRNA synthetase in complex with Trp
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2qui:
Crystal structures of human tryptophanyl-tRNA synthetase in complex with Tryptophanamide and ATP
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2quj:
Crystal structures of human tryptophanyl-tRNA synthetase in complex with TrpAMP
Method: X-RAY DIFFRACTION / Resolution: 2.42 Å

PDB-2quk:
Crystal structures of human tryptophanyl-tRNA synthetase in complex with ATP(putative)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-TRP:
TRYPTOPHAN

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-LTN:
L-TRYPTOPHANAMIDE

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-CL:
Unknown entry

ChemComp-TYM:
TRYPTOPHANYL-5'AMP

ChemComp-GOL:
GLYCEROL

Source
  • homo sapiens (human)
KeywordsLIGASE / Aminoacyl-tRNA synthetase / Rossmann fold / induced-fit mechnism / ATP-binding / Cytoplasm / Nucleotide-binding / Protein biosynthesis

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