1ybv

From Proteopedia

Revision as of 14:28, 30 October 2007

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

Overview

BACKGROUND: 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. RESULTS: Crystallographic, analysis showed four identical subunits of THNR to form a tetramer with, 222 symmetry. The enzyme subunit consists of a single domain comprising a, seven-stranded beta sheet flanked by eight alpha helices; the subunit, contains a dinucleotide-binding fold which binds the coenzyme, NADPH., ... [(full description)]

About this Structure

1YBV is a [Single protein] structure of sequence from [Magnaporthe grisea] with NDP and BEA as [ligands]. Active as [Transferred entry: 1.1.1.252], with EC number [1.3.1.50]. Structure known Active Sites: A1, A2, B1 and B2. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor., Andersson A, Jordan D, Schneider G, Lindqvist Y, Structure. 1996 Oct 15;4(10):1161-70. PMID:8939741

Page seeded by OCA on Tue Oct 30 16:33:15 2007