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1phz

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Revision as of 07:31, 15 February 2018

STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE

Structural highlights

1phz is a 1 chain structure with sequence from Buffalo rat. The January 2005 RCSB PDB Molecule of the Month feature on Phenylalanine Hydroxylase by Shuchismita Dutta and David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Phenylalanine 4-monooxygenase, with EC number 1.14.16.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kobe B, Jennings IG, House CM, Michell BJ, Goodwill KE, Santarsiero BD, Stevens RC, Cotton RG, Kemp BE. Structural basis of autoregulation of phenylalanine hydroxylase. Nat Struct Biol. 1999 May;6(5):442-8. PMID:10331871 doi:10.1038/8247

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE==
 <StructureSection load='1phz' size='340' side='right' caption='[[1phz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1phz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1phz RCSB], [http://www.ebi.ac.uk/pdbsum/1phz PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1phz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1phz RCSB], [http://www.ebi.ac.uk/pdbsum/1phz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1phz ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ph/1phz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ph/1phz_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 ==See Also==
-*[[Hydroxylase|Hydroxylase]]
+*[[Journal:Proteins:2|Journal:Proteins:2]]
+*[[Protein Stability and in Vivo Concentration of Missense Mutations in Phenylalanine Hydroxylase|Protein Stability and in Vivo Concentration of Missense Mutations in Phenylalanine Hydroxylase]]
 == References ==
 <references/>

1phz

From Proteopedia

Revision as of 07:31, 15 February 2018

STRUCTURE OF PHOSPHORYLATED PHENYLALANINE HYDROXYLASE

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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