1YBV

STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR

1YBV の概要

• エントリーDOI: 10.2210/pdb1ybv/pdb
• 分子名称: TRIHYDROXYNAPHTHALENE REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 5-METHYL-1,2,4-TRIAZOLO[3,4-B]BENZOTHIAZOLE (3 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Magnaporthe grisea
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62174.62

構造登録者

Andersson, A.,Schneider, G.,Lindqvist, Y. (登録日: 1996-09-23, 公開日: 1997-10-15, 最終更新日: 2024-02-14)

主引用文献

Andersson, A.,Jordan, D.,Schneider, G.,Lindqvist, Y.
Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor.
Structure, 4:1161-1170, 1996

PubMed Abstract: The enzyme 1,3,8-trihydroxynaphthalene reductase (THNR) catalyzes an essential reaction in the biosynthesis of melanin, a black pigment crucial for the pathogenesis of the rice blast fungus, Magnaporthe grisea. The enzyme is the biochemical target of several commercially important fungicides which are used to prevent blast disease in rice plants. We have determined the structure of the ternary complex of THNR with bound NADPH and a fungicide, tricyclazole.

PubMed: 8939741
DOI: 10.1016/S0969-2126(96)00124-4

実験手法

X-RAY DIFFRACTION (2.8 Å)