2bkj
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NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI COMPLEXED WITH NAD+
OverviewOverview
The 2.1 A resolution crystal structure of flavin reductase P with the, inhibitor nicotinamide adenine dinucleotide (NAD) bound in the active site, has been determined. NAD adopts a novel, folded conformation in which the, nicotinamide and adenine rings stack in parallel with an inter-ring, distance of 3.6 A. The pyrophosphate binds next to the flavin cofactor, isoalloxazine, while the stacked nicotinamide/adenine moiety faces away, from the flavin. The observed NAD conformation is quite different from the, extended conformations observed in other enzyme/NAD(P) structures;, however, it resembles the conformation proposed for NAD in solution. The, flavin reductase P/NAD structure provides new information about the, conformational diversity of NAD, which is important for understanding, catalysis. This structure offers the first crystallographic evidence of a, folded NAD with ring stacking, and it is the first enzyme structure, containing an FMN cofactor interacting with NAD(P). Analysis of the, structure suggests a possible dynamic mechanism underlying NADPH substrate, specificity and product release that involves unfolding and folding of, NADP(H).
About this StructureAbout this Structure
2BKJ is a Single protein structure of sequence from Vibrio harveyi with FMN and NAD as ligands. Active as FMN reductase, with EC number 1.5.1.29 Full crystallographic information is available from OCA.
ReferenceReference
Unusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase P., Tanner JJ, Tu SC, Barbour LJ, Barnes CL, Krause KL, Protein Sci. 1999 Sep;8(9):1725-32. PMID:10493573
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