2phm
From Proteopedia
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STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED
Overview
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.
About this Structure
2PHM is a Single protein structure of sequence from Rattus norvegicus with FE as ligand. Active as Phenylalanine 4-monooxygenase, with EC number 1.14.16.1 Full crystallographic information is available from OCA.
Reference
Structural basis of autoregulation of phenylalanine hydroxylase., Kobe B, Jennings IG, House CM, Michell BJ, Goodwill KE, Santarsiero BD, Stevens RC, Cotton RG, Kemp BE, Nat Struct Biol. 1999 May;6(5):442-8. PMID:10331871
Page seeded by OCA on Wed Nov 21 13:32:16 2007
