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Structure paper

TitleCrystal structures of Saccharomyces cerevisiae tryptophanyl-tRNA synthetase: new insights into the mechanism of tryptophan activation and implications for anti-fungal drug design
Journal, issue, pagesNucleic Acids Res., Vol. 38, Page 3399-3413, Year 2010
Publish dateNov 24, 2009 (structure data deposition date)
AuthorsZhou, M. / Dong, X. / Shen, N. / Zhong, C. / Ding, J.
External linksNucleic Acids Res. / PubMed:20123733
MethodsX-ray diffraction
Resolution2.1 - 3 Å
Structure data

PDB-3kt0:
Crystal structure of S. cerevisiae tryptophanyl-tRNA synthetase.
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3kt3:
Crystal structure of S. cerevisiae tryptophanyl-tRNA synthetase in complex with TrpAMP
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-3kt6:
Crystal structure of S. cerevisiae tryptophanyl-tRNA synthetase in complex with Trp
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3kt8:
Crystal structure of S. cerevisiae tryptophanyl-tRNA synthetase in complex with L-tryptophanamide
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-EMN:
(2S)-1-{[(2S)-3-(2-methoxyethoxy)-2-methylpropyl]oxy}propan-2-amine

ChemComp-HOH:
WATER

ChemComp-TYM:
TRYPTOPHANYL-5'AMP

ChemComp-SO4:
SULFATE ION

ChemComp-TRP:
TRYPTOPHAN

ChemComp-LTN:
L-TRYPTOPHANAMIDE

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsLIGASE / tryptophanyl-tRNA synthetase / Rossmann fold / S. cerevisiae / Aminoacyl-tRNA synthetase / ATP-binding / Cytoplasm / Nucleotide-binding / Protein biosynthesis / sulfate ion / amino acid activation / catalytic mechanism / tryptophanamide

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