Motion in Phenylalanine Hydroxylase [pah]

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Classification [D-s-2]

Structures
1PAH

Description
Phenylalanine hydroxylase catalyse the hydroxylation of L-Phenylalanine to L-Tyrosine in the presence of the cofactor tetrahydrobiopterin and dioxygen. This movie illustrates the large-scale structural changes that are observed upon binding of the substrate analogue thienylalanine to the catalytic domain (residues 103-427) of phenylalanine hydroxylase. The conformational change involves a relocation of loop residue Tyr138 from a surface position in the substrate-free enzyme to a buried position in the active site in the substrate-bound enzyme.

References
H Erlandsen, F Fusetti, A Martinez, E Hough, T Flatmark, R C Stevens (1997). Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat Struct Biol, 4:995-1000 [Medline info for 9406548]

GO terms associated with structures
Molecular functionmonooxygenase activity, phenylalanine 4-monooxygenase activity, amino acid binding, iron ion binding
Biological processmetabolism, aromatic amino acid family metabolism, L-phenylalanine catabolism

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
phenylalanine hydroxylase 1pah [ A ] upload [ A ] 307

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
484471-1973 Phenylalanine Hydroxylase upload [ A ] upload [ A ] 307
571404-31794 Phenylalanine Hydroxylase upload [ A ] upload [ A ] 308


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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu