Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase

Bostjan Kobe, Ian G. Jennings, Colin M. House, Susanne C. Feil, Belinda J. Michell, Tony Tiganis, Michael W. Parker, Richard G.H. Cotton, Bruce E. Kemp

Research output: Contribution to journalArticleResearchpeer-review

19 Citations (Scopus)

Abstract

Phenylalanine hydroxylase is regulated in a complex manner, including activation by phosphorylation. It is normally found as an equilibrium of dimeric and tetrameric species, with the tetramer thought to be the active form. We converted the protein to the dimeric form by deleting the C-terminal 24 residues and show that the truncated protein remains active and regulated by phosphorylation. This indicates that changes in the tetrameric quaternary structure of phenylalanine hydroxylase are not required for enzyme activation. Truncation also facilitates crystallization of both phosphorylated and dephosphorylated forms of the enzyme.

Original languageEnglish
Pages (from-to)1352-1357
Number of pages6
JournalProtein Science
Volume6
Issue number6
DOIs
Publication statusPublished - 1 Jan 1997
Externally publishedYes

Keywords

  • Crystallization
  • Phenylalanine hydroxylase
  • Protein phosphorylation
  • Quaternary structure
  • X-ray crystallography

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