1vfr

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spinqualitylabelsall models 1vfr, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE MAJOR NAD(P)H:FMN OXIDOREDUCTASE FROM VIBRIO FISCHERI

Overview

We have solved the crystal structure of FRase I, the major NAD(P)H:FMN, oxidoreductase of Vibrio fischeri, by the multiple isomorphous replacement, method (MIR) at 1.8 A resolution with the conventional R factor of 0.187., The crystal structure of FRase I complexed with its competitive inhibitor, dicoumarol, has also been solved at 2.2 A resolution with the conventional, R factor of 0.161. FRase I is a homodimer, having one FMN cofactor per, subunit, which is situated at the interface of two subunits. The overall, fold can be divided into two domains; 80% of the residues form a rigid, core and the remaining, a small flexible domain. The overall core folding, is similar to those of an NADPH-dependent flavin reductase of Vibrio, harveyi (FRP) and the NADH oxidase of Thermus thermophilus ... [(full description)]

About this Structure

1VFR is a [Single protein] structure of sequence from [Vibrio fischeri] with FMN as [ligand]. Active as [[1]], with EC number [1.6.8.1]. Full crystallographic information is available from [OCA].

Reference

1.8 A crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins., Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M, J Mol Biol. 1998 Jul 10;280(2):259-73. PMID:9654450

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