2PHM

STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED

2PHM の概要

• エントリーDOI: 10.2210/pdb2phm/pdb
• 分子名称: PROTEIN (PHENYLALANINE-4-HYDROXYLASE), FE (III) ION (3 entities in total)
• 機能のキーワード: phenylalanine hydroxylase, aromatic amino acid hydroxylase, phosphorylation, intrasteric regulation, allosteric regulation, oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49385.39

構造登録者

Kobe, B.,Jennings, I.G.,House, C.M.,Michell, B.J.,Cotton, R.G.,Kemp, B.E. (登録日: 1998-11-11, 公開日: 1999-04-30, 最終更新日: 2024-04-03)

主引用文献

Kobe, B.,Jennings, I.G.,House, C.M.,Michell, B.J.,Goodwill, K.E.,Santarsiero, B.D.,Stevens, R.C.,Cotton, R.G.,Kemp, B.E.
Structural basis of autoregulation of phenylalanine hydroxylase.
Nat.Struct.Biol., 6:442-448, 1999

PubMed Abstract: Phenylalanine hydroxylase converts phenylalanine to tyrosine, a rate-limiting step in phenylalanine catabolism and protein and neurotransmitter biosynthesis. It is tightly regulated by the substrates phenylalanine and tetrahydrobiopterin and by phosphorylation. We present the crystal structures of dephosphorylated and phosphorylated forms of a dimeric enzyme with catalytic and regulatory properties of the wild-type protein. The structures reveal a catalytic domain flexibly linked to a regulatory domain. The latter consists of an N-terminal autoregulatory sequence (containing Ser 16, which is the site of phosphorylation) that extends over the active site pocket, and an alpha-beta sandwich core that is, unexpectedly, structurally related to both pterin dehydratase and the regulatory domains of metabolic enzymes. Phosphorylation has no major structural effects in the absence of phenylalanine, suggesting that phenylalanine and phosphorylation act in concert to activate the enzyme through a combination of intrasteric and possibly allosteric mechanisms.

PubMed: 10331871
DOI: 10.1038/8247

実験手法

X-RAY DIFFRACTION (2.6 Å)