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Structure paper

TitleGenetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader.
Journal, issue, pagesChem. Commun. (Camb. ), Vol. 52, Page 12606-12609, Year 2016
Publish dateMay 18, 2016 (structure data deposition date)
AuthorsLee, Y.J. / Schmidt, M.J. / Tharp, J.M. / Weber, A. / Koenig, A.L. / Zheng, H. / Gao, J. / Waters, M.L. / Summerer, D. / Liu, W.R.
External linksChem. Commun. (Camb. ) / PubMed:27711380
MethodsX-ray diffraction
Resolution1.499 - 1.95 Å
Structure data

PDB-5k1p:
Catalytic domain of polyspecific pyrrolysyl-tRNA synthetase mutant N346A/C348A in complex with AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 1.499 Å

PDB-5k1x:
Catalytic domain of polyspecific pyrrolysyl-tRNA synthetase mutant Y306A/N346A/C348A/Y384F in complex with AMPPNP
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-CL:
Unknown entry

Source
  • methanosarcina mazei (archaea)
KeywordsLIGASE / protein engineering / aminoacyl-tRNA synthetase / noncanonical amino acids

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