2phm
From Proteopedia
(New page: 200px<br /><applet load="2phm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2phm, resolution 2.60Å" /> '''STRUCTURE OF PHENYLA...) |
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| - | [[Image:2phm.jpg|left|200px]]<br /><applet load="2phm" size=" | + | [[Image:2phm.jpg|left|200px]]<br /><applet load="2phm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2phm, resolution 2.60Å" /> | caption="2phm, resolution 2.60Å" /> | ||
'''STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED'''<br /> | '''STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phenylalanine hydroxylase converts phenylalanine to tyrosine, a | + | 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== | ==About this Structure== | ||
| - | 2PHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 2PHM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PHM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cotton, R | + | [[Category: Cotton, R G.]] |
| - | [[Category: House, C | + | [[Category: House, C M.]] |
| - | [[Category: Jennings, I | + | [[Category: Jennings, I G.]] |
| - | [[Category: Kemp, B | + | [[Category: Kemp, B E.]] |
[[Category: Kobe, B.]] | [[Category: Kobe, B.]] | ||
| - | [[Category: Michell, B | + | [[Category: Michell, B J.]] |
[[Category: FE]] | [[Category: FE]] | ||
[[Category: allosteric regulation]] | [[Category: allosteric regulation]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:29:29 2008'' |
Revision as of 16:29, 21 February 2008
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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 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
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