1YBV

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

Summary for 1YBV

• Entry DOI: 10.2210/pdb1ybv/pdb
• Descriptor: TRIHYDROXYNAPHTHALENE REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 5-METHYL-1,2,4-TRIAZOLO[3,4-B]BENZOTHIAZOLE (3 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Magnaporthe grisea
• Total number of polymer chains: 2
• Total formula weight: 62174.62

Authors

Andersson, A.,Schneider, G.,Lindqvist, Y. (deposition date: 1996-09-23, release date: 1997-10-15, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)