1toh
From Proteopedia
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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 ... [(full description)]
About this Structure
1TOH is a [Single protein] structure of sequence from [Rattus norvegicus] with FE as [ligand]. Active as [[1]], with EC number [1.14.16.2]. 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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