2MDA

The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase

2MDA の概要

• エントリーDOI: 10.2210/pdb2mda/pdb
• NMR情報: BMRB: 19482
• 分子名称: Tyrosine 3-monooxygenase (1 entity in total)
• 機能のキーワード: tyrosine hydroxylase, regulation, act domain, oxidoreductase
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20971.73

構造登録者

Zhang, S.,Huang, T.,Hinck, A.,Fitzpatrick, P. (登録日: 2013-09-08, 公開日: 2014-01-01, 最終更新日: 2024-05-01)

主引用文献

Zhang, S.,Huang, T.,Ilangovan, U.,Hinck, A.P.,Fitzpatrick, P.F.
The solution structure of the regulatory domain of tyrosine hydroxylase.
J.Mol.Biol., 426:1483-1497, 2014

PubMed Abstract: Tyrosine hydroxylase (TyrH) catalyzes the hydroxylation of tyrosine to form 3,4-dihydroxyphenylalanine in the biosynthesis of the catecholamine neurotransmitters. The activity of the enzyme is regulated by phosphorylation of serine residues in a regulatory domain and by binding of catecholamines to the active site. Available structures of TyrH lack the regulatory domain, limiting the understanding of the effect of regulation on structure. We report the use of NMR spectroscopy to analyze the solution structure of the isolated regulatory domain of rat TyrH. The protein is composed of a largely unstructured N-terminal region (residues 1-71) and a well-folded C-terminal portion (residues 72-159). The structure of a truncated version of the regulatory domain containing residues 65-159 has been determined and establishes that it is an ACT domain. The isolated domain is a homodimer in solution, with the structure of each monomer very similar to that of the core of the regulatory domain of phenylalanine hydroxylase. Two TyrH regulatory domain monomers form an ACT domain dimer composed of a sheet of eight strands with four α-helices on one side of the sheet. Backbone dynamic analyses were carried out to characterize the conformational flexibility of TyrH65-159. The results provide molecular details critical for understanding the regulatory mechanism of TyrH.

PubMed: 24361276
DOI: 10.1016/j.jmb.2013.12.015

実験手法

SOLUTION NMR