1phz: Difference between revisions
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|PDB= 1phz |SIZE=350|CAPTION= <scene name='initialview01'>1phz</scene>, resolution 2.20Å | |PDB= 1phz |SIZE=350|CAPTION= <scene name='initialview01'>1phz</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Phenylalanine_4-monooxygenase Phenylalanine 4-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_4-monooxygenase Phenylalanine 4-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.1 1.14.16.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1phz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1phz OCA], [http://www.ebi.ac.uk/pdbsum/1phz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1phz RCSB]</span> | |||
}} | }} | ||
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[[Category: Kobe, B.]] | [[Category: Kobe, B.]] | ||
[[Category: Michell, B J.]] | [[Category: Michell, B J.]] | ||
[[Category: allosteric regulation]] | [[Category: allosteric regulation]] | ||
[[Category: aromatic amino acid hydroxylase]] | [[Category: aromatic amino acid hydroxylase]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:59:53 2008'' | ||
Revision as of 22:59, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | |||||||
| Activity: | Phenylalanine 4-monooxygenase, with EC number 1.14.16.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE
OverviewOverview
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 StructureAbout this Structure
1PHZ is a Single protein structure of sequence from Rattus norvegicus. The following page contains interesting information on the relation of 1PHZ with [Phenylalanine Hydroxylase]. Full crystallographic information is available from OCA.
ReferenceReference
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
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