Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium

Dysfunction of human phenylalanine hydroxylase (hPAH, EC 1.14.16.1) is the primary cause of phenylketonuria, the most common inborn error of amino acid metabolism. The dynamic domain rearrangements of this multimeric protein have thwarted structural study of the full-length form for decades, until n...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 294; no. 26; pp. 10131 - 10145
Main Authors:	Arturo, Emilia C., Gupta, Kushol, Hansen, Michael R., Borne, Elias, Jaffe, Eileen K.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 28-06-2019 American Society for Biochemistry and Molecular Biology
Subjects:	ACT domain Allosteric Regulation Biophysics Crystallography, X-Ray Humans inborn error of metabolism Models, Molecular Molecular Biophysics Phenylalanine - chemistry Phenylalanine - metabolism phenylalanine hydroxylase Phenylalanine Hydroxylase - chemistry Phenylalanine Hydroxylase - metabolism phenylketonuria Protein Binding protein conformation Protein Multimerization Protein Structure, Quaternary resting-state structure small-angle X-ray scattering (SAXS) structural biology structural modeling X-ray crystallography X-ray crystallography small-angle X-ray scattering (SAXS) phenylalanine hydroxylase protein conformation resting-state structure structural biology structural modeling allosteric regulation inborn error of metabolism phenylketonuria ACT domain
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