2phm: Difference between revisions

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-[[Image:2phm.jpg|left|200px]]
- {{Structure
+==STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED==
-|PDB= 2phm |SIZE=350|CAPTION= <scene name='initialview01'>2phm</scene>, resolution 2.60&Aring;
+<StructureSection load='2phm' size='340' side='right'caption='[[2phm]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene>
+<table><tr><td colspan='2'>[[2phm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PHM FirstGlance]. <br>
-|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]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2phm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2phm OCA], [https://pdbe.org/2phm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2phm RCSB], [https://www.ebi.ac.uk/pdbsum/2phm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2phm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PH4H_RAT PH4H_RAT]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ph/2phm_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2phm ConSurf].
+<div style="clear:both"></div>
-'''STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED'''
+==See Also==
+*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
-==About this Structure==
-PHM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PHM 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:[http://www.ncbi.nlm.nih.gov/pubmed/10331871 10331871]
-[[Category: Phenylalanine 4-monooxygenase]]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Cotton RG]]
-[[Category: Cotton, R G.]]
+[[Category: House CM]]
-[[Category: House, C M.]]
+[[Category: Jennings IG]]
-[[Category: Jennings, I G.]]
+[[Category: Kemp BE]]
-[[Category: Kemp, B E.]]
+[[Category: Kobe B]]
-[[Category: Kobe, B.]]
+[[Category: Michell BJ]]
-[[Category: Michell, B J.]]
-[[Category: FE]]
-[[Category: allosteric regulation]]
-[[Category: aromatic amino acid hydroxylase]]
-[[Category: intrasteric regulation]]
-[[Category: phenylalanine hydroxylase]]
-[[Category: phosphorylation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:13:05 2008''