1toh

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[[Image:1toh.gif|left|200px]]
 
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{{Structure
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==TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT==
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|PDB= 1toh |SIZE=350|CAPTION= <scene name='initialview01'>1toh</scene>, resolution 2.30&Aring;
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<StructureSection load='1toh' size='340' side='right'caption='[[1toh]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE= <scene name='pdbsite=FE:Fe+Binding+Site'>FE</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene>
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<table><tr><td colspan='2'>[[1toh]] 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=1TOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TOH FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Tyrosine_3-monooxygenase Tyrosine 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.16.2 1.14.16.2]
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</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>
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|GENE=
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<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>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1toh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1toh OCA], [https://pdbe.org/1toh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1toh RCSB], [https://www.ebi.ac.uk/pdbsum/1toh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1toh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TY3H_RAT TY3H_RAT] Plays an important role in the physiology of adrenergic neurons.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/to/1toh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1toh ConSurf].
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<div style="clear:both"></div>
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'''TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT'''
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==See Also==
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*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Tyrosine hydroxylase (TyrOH) catalyzes the conversion of tyrosine to L-DOPA, the rate-limiting step in the biosynthesis of the catecholamines dopamine, adrenaline, and noradrenaline. TyrOH is highly homologous in terms of both protein sequence and catalytic mechanism to phenylalanine hydroxylase (PheOH) and tryptophan hydroxylase (TrpOH). The crystal structure of the catalytic and tetramerization domains of TyrOH reveals a novel alpha-helical basket holding the catalytic iron and a 40 A long anti-parallel coiled coil which forms the core of the tetramer. The catalytic iron is located 10 A below the enzyme surface in a 17 A deep active site pocket and is coordinated by the conserved residues His 331, His 336 and Glu 376. The structure provides a rationale for the effect of point mutations in TyrOH that cause L-DOPA responsive parkinsonism and Segawa's syndrome. The location of 112 different point mutations in PheOH that lead to phenylketonuria (PKU) are predicted based on the TyrOH structure.
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[[Category: Large Structures]]
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==About this Structure==
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1TOH 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=1TOH OCA].
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==Reference==
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Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases., Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens RC, Nat Struct Biol. 1997 Jul;4(7):578-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9228951 9228951]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Goodwill KE]]
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[[Category: Tyrosine 3-monooxygenase]]
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[[Category: Sabatier C]]
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[[Category: Goodwill, K E.]]
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[[Category: Stevens RC]]
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[[Category: Sabatier, C.]]
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[[Category: Stevens, R C.]]
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[[Category: FE]]
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[[Category: hydroxylase]]
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[[Category: neurotransmitter biosynthesis]]
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[[Category: non-heme iron]]
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[[Category: pterin co-substrate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:21:07 2008''
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Current revision

TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT

PDB ID 1toh

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