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Structure paper

TitleThe Double-Length Tyrosyl-tRNA Synthetase from the Eukaryote Leishmania major Forms an Intrinsically Asymmetric Pseudo-Dimer.
Journal, issue, pagesJ. Mol. Biol., Vol. 409, Page 159-176, Year 2011
Publish dateSep 28, 2010 (structure data deposition date)
AuthorsLarson, E.T. / Kim, J.E. / Castaneda, L.J. / Napuli, A.J. / Zhang, Z. / Fan, E. / Zucker, F.H. / Verlinde, C.L. / Buckner, F.S. / Van Voorhis, W.C. ...Larson, E.T. / Kim, J.E. / Castaneda, L.J. / Napuli, A.J. / Zhang, Z. / Fan, E. / Zucker, F.H. / Verlinde, C.L. / Buckner, F.S. / Van Voorhis, W.C. / Hol, W.G. / Merritt, E.A.
External linksJ. Mol. Biol. / PubMed:21420975
MethodsX-ray diffraction
Resolution2.89 - 3.13 Å
Structure data

PDB-3p0h:
Leishmania major Tyrosyl-tRNA synthetase in complex with fisetin, cubic crystal form
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-3p0i:
Leishmania major Tyrosyl-tRNA synthetase in complex with tyrosinol, cubic crystal form
Method: X-RAY DIFFRACTION / Resolution: 3.13 Å

PDB-3p0j:
Leishmania major Tyrosyl-tRNA synthetase in complex with tyrosinol, triclinic crystal form 1
Method: X-RAY DIFFRACTION / Resolution: 2.89 Å

Chemicals

ChemComp-FSE:
3,7,3',4'-TETRAHYDROXYFLAVONE

ChemComp-TYE:
4-[(2S)-2-amino-3-hydroxypropyl]phenol

ChemComp-NA:
Unknown entry

Source
  • leishmania major (eukaryote)
KeywordsLIGASE / aminoacyl-tRNA synthetase / tRNA ligase / aaRS / TyrRS / pseudodimer / translation / ATP-binding / nucleotide-binding / Structural Genomics / Medical Structural Genomics of Pathogenic Protozoa / MSGPP

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