1toh

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[[Image:1toh.gif|left|200px]]
[[Image:1toh.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1toh |SIZE=350|CAPTION= <scene name='initialview01'>1toh</scene>, resolution 2.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1toh", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=FE:Fe+Binding+Site'>FE</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1toh| PDB=1toh | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1toh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1toh OCA], [http://www.ebi.ac.uk/pdbsum/1toh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1toh RCSB]</span>
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}}
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'''TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT'''
'''TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT'''
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[[Category: Sabatier, C.]]
[[Category: Sabatier, C.]]
[[Category: Stevens, R C.]]
[[Category: Stevens, R C.]]
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[[Category: hydroxylase]]
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[[Category: Hydroxylase]]
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[[Category: neurotransmitter biosynthesis]]
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[[Category: Neurotransmitter biosynthesis]]
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[[Category: non-heme iron]]
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[[Category: Non-heme iron]]
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[[Category: pterin co-substrate]]
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[[Category: Pterin co-substrate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:11:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:58:55 2008''
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Revision as of 07:11, 3 May 2008

Image:1toh.gif

Template:STRUCTURE 1toh

TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT


Overview

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.

About this Structure

1TOH is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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:9228951 Page seeded by OCA on Sat May 3 10:11:18 2008

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