1phz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1phz.jpg|left|200px]]<br /><applet load="1phz" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1phz.jpg|left|200px]]
-
caption="1phz, resolution 2.20&Aring;" />
+
 
-
'''STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE'''<br />
+
{{Structure
 +
|PDB= 1phz |SIZE=350|CAPTION= <scene name='initialview01'>1phz</scene>, resolution 2.20&Aring;
 +
|SITE=
 +
|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]
 +
|GENE=
 +
}}
 +
 
 +
'''STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1PHZ 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]. The following page contains interesting information on the relation of 1PHZ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb61_1.html Phenylalanine Hydroxylase]]. 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=1PHZ OCA].
+
1PHZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. The following page contains interesting information on the relation of 1PHZ with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb61_1.html Phenylalanine Hydroxylase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PHZ OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10331871 10331871]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/10331871 10331871]
[[Category: Phenylalanine 4-monooxygenase]]
[[Category: Phenylalanine 4-monooxygenase]]
[[Category: Phenylalanine Hydroxylase]]
[[Category: Phenylalanine Hydroxylase]]
Line 28: Line 37:
[[Category: phosphorylation]]
[[Category: phosphorylation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:28:58 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:24:32 2008''

Revision as of 11:24, 20 March 2008

Image:1phz.jpg


PDB ID 1phz

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Activity: Phenylalanine 4-monooxygenase, with EC number 1.14.16.1
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE


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

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.

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 Thu Mar 20 13:24:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1phz"
Personal tools