2toh

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2toh, resolution 2.30Å

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TYROSINE HYDROXYLASE CATALYTIC AND TETRAMERIZATION DOMAINS FROM RAT

Overview

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 ... [(full description)]

About this Structure

2TOH is a [Single protein] structure of sequence from [Rattus norvegicus] with FE, CL and HBI as [ligands]. The following page contains interesting information on the relation of 2TOH with [Phenylalanine Hydroxylase]. Active as [Tyrosine 3-monooxygenase], with EC number [1.14.16.2]. Structure known Active Sites: FE and MTY. Full crystallographic information is available from [OCA].

Reference

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:9753429

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