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TitleDomain Movements upon Activation of Phenylalanine Hydroxylase Characterized by Crystallography and Chromatography-Coupled Small-Angle X-ray Scattering.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 138, Page 6506-6516, Year 2016
Publish dateOct 27, 2015 (structure data deposition date)
AuthorsMeisburger, S.P. / Taylor, A.B. / Khan, C.A. / Zhang, S. / Fitzpatrick, P.F. / Ando, N.
External linksJ. Am. Chem. Soc. / PubMed:27145334
MethodsX-ray diffraction
Resolution2.5 - 3.6 Å
Structure data

PDB-5egq:
Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues 25-453
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5fgj:
Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-FE:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • rattus norvegicus (Norway rat)
KeywordsOXIDOREDUCTASE / hydroxylase / phenylketonuria / PKU mutation / allostery / ACT domain

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