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1toh

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{{STRUCTURE_1toh| PDB=1toh | SCENE= }}
{{STRUCTURE_1toh| PDB=1toh | SCENE= }}
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'''TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT'''
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===TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 9228951 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9228951}}
==About this Structure==
==About this Structure==
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[[Category: Non-heme iron]]
[[Category: Non-heme iron]]
[[Category: Pterin co-substrate]]
[[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 Tue Jul 29 15:17:52 2008''

Revision as of 12:17, 29 July 2008

Image:1toh.png

Template:STRUCTURE 1toh

TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT

Template:ABSTRACT PUBMED 9228951

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

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