1MLW

Crystal structure of human tryptophan hydroxylase with bound 7,8-dihydro-L-biopterin cofactor and Fe(III)

1MLW の概要

• エントリーDOI: 10.2210/pdb1mlw/pdb
• 分子名称: Tryptophan 5-monooxygenase, FE (III) ION, 7,8-DIHYDROBIOPTERIN, ... (4 entities in total)
• 機能のキーワード: aromatic amino acid hydroxylase catalytic domain fold, oxidoreductase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34936.60

構造登録者

Wang, L.,Erlandsen, H.,Haavik, J.,Knappskog, P.M.,Stevens, R.C. (登録日: 2002-08-31, 公開日: 2002-12-18, 最終更新日: 2024-02-14)

主引用文献

Wang, L.,Erlandsen, H.,Haavik, J.,Knappskog, P.M.,Stevens, R.C.
Three-dimensional structure of human tryptophan hydroxylase and its implications for the biosynthesis of the neurotransmitters serotonin and melatonin
Biochemistry, 41:12569-12574, 2002

PubMed Abstract: Tryptophan hydroxylase oxidizes L-tryptophan to 5-hydroxy-L-tryptophan in the rate-determining step of serotonin biosynthesis. We have determined the X-ray crystal structure (1.7 A) of a truncated functional form of human tryptophan hydroxylase with the bound cofactor analogue 7,8-dihydro-L-biopterin, providing the first atomic-resolution information for the catalytic domain of this important enzyme. Comparison of the three-dimensional structures of all three members of the aromatic amino acid hydroxylase family--tyrosine hydroxylase, phenylalanine hydroxylase, and tryptophan hydroxylase--reveals important differences at the active sites.

PubMed: 12379098
DOI: 10.1021/bi026561f

実験手法

X-RAY DIFFRACTION (1.71 Å)