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New page: left|200px<br /> <applet load="2toh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2toh, resolution 2.30Å" /> '''TYROSINE HYDROXYLAS...
 
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[[Image:2toh.gif|left|200px]]<br />
<applet load="2toh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2toh, resolution 2.30&Aring;" />
'''TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT'''<br />


==Overview==
==TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT==
TyrOH is a non-heme iron enzyme which uses molecular oxygen to hydroxylate, tyrosine to form L-dihydroxyphenylalanine (L-DOPA), and, tetrahydrobiopterin to form 4a-hydroxybiopterin, in the rate-limiting step, of the catecholamine biosynthetic pathway. The 2.3 A crystal structure of, the catalytic and tetramerization domains of rat tyrosine hydroxylase, (TyrOH) in the presence of the cofactor analogue 7,8-dihydrobiopterin and, iron shows the mode of pterin binding and the proximity of its, hydroxylated 4a carbon to the required iron. The pterin binds on one face, of the large active-site cleft, forming an aromatic pi-stacking, interaction with Phe300. This phenylalanine residue of TyrOH is found to, be hydroxylated in the meta position, most likely through an autocatalytic, process, and to ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9753429 (full description)]]
<StructureSection load='2toh' size='340' side='right'caption='[[2toh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2toh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. The January 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Phenylalanine Hydroxylase''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_1 10.2210/rcsb_pdb/mom_2005_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TOH 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene>, <scene name='pdbligand=MTY:META-TYROSINE'>MTY</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=2toh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2toh OCA], [https://pdbe.org/2toh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2toh RCSB], [https://www.ebi.ac.uk/pdbsum/2toh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2toh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TY3H_RAT TY3H_RAT] Plays an important role in the physiology of adrenergic neurons.
== 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/to/2toh_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=2toh ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2TOH 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, CL and HBI as [[http://en.wikipedia.org/wiki/ligands ligands]]. The following page contains interesting information on the relation of 2TOH 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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.2 1.14.16.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2TOH OCA]].
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 A resolution: self-hydroxylation of Phe300 and the pterin-binding site., Goodwill KE, Sabatier C, Stevens RC, Biochemistry. 1998 Sep 29;37(39):13437-45. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9753429 9753429]
[[Category: Large Structures]]
[[Category: Phenylalanine Hydroxylase]]
[[Category: Phenylalanine Hydroxylase]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Goodwill KE]]
[[Category: Goodwill, K.E.]]
[[Category: Sabatier C]]
[[Category: Sabatier, C.]]
[[Category: Stevens RC]]
[[Category: Stevens, R.C.]]
[[Category: CL]]
[[Category: FE]]
[[Category: HBI]]
[[Category: catecholamine biosynthesis]]
[[Category: hydroxylase]]
[[Category: neurotransmitter biosynthesis]]
[[Category: non-heme iron]]
[[Category: oxidoreductase]]
[[Category: pterin co-substrate]]
 
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