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-Structure paper
Title | The Double-Length Tyrosyl-tRNA Synthetase from the Eukaryote Leishmania major Forms an Intrinsically Asymmetric Pseudo-Dimer. |
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Journal, issue, pages | J. Mol. Biol., Vol. 409, Page 159-176, Year 2011 |
Publish date | Sep 28, 2010 (structure data deposition date) |
Authors | 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. ...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 links | J. Mol. Biol. / PubMed:21420975 |
Methods | X-ray diffraction |
Resolution | 2.89 - 3.13 Å |
Structure data | PDB-3p0h: PDB-3p0i: PDB-3p0j: |
Chemicals | ChemComp-FSE: ChemComp-TYE: ChemComp-NA: |
Source |
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Keywords | LIGASE / aminoacyl-tRNA synthetase / tRNA ligase / aaRS / TyrRS / pseudodimer / translation / ATP-binding / nucleotide-binding / Structural Genomics / Medical Structural Genomics of Pathogenic Protozoa / MSGPP |