2phm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2phm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2phm, resolution 2.60&Aring;" /> '''STRUCTURE OF PHENYLA...)
Current revision (06:30, 3 April 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2phm.jpg|left|200px]]<br /><applet load="2phm" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2phm, resolution 2.60&Aring;" />
 
-
'''STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED'''<br />
 
-
==Overview==
+
==STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED==
-
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.
+
<StructureSection load='2phm' size='340' side='right'caption='[[2phm]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<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>
 +
</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>
 +
<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>
-
==About this Structure==
+
==See Also==
-
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PHM OCA].
+
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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]
+
[[Category: Large Structures]]
-
[[Category: Phenylalanine 4-monooxygenase]]
+
[[Category: Rattus norvegicus]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:32:16 2007''
+

Current revision

STRUCTURE OF PHENYLALANINE HYDROXYLASE DEPHOSPHORYLATED

PDB ID 2phm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2phm"
Personal tools