2BKJ

NADPH:FMN OXIDOREDUCTASE FROM VIBRIO HARVEYI COMPLEXED WITH NAD+

Summary for 2BKJ

• Entry DOI: 10.2210/pdb2bkj/pdb
• Descriptor: FLAVIN REDUCTASE, FLAVIN MONONUCLEOTIDE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, frp
• Biological source: Vibrio harveyi
• Total number of polymer chains: 2
• Total formula weight: 54243.35

Authors

Tanner, J.J.,TU, S.-C.,Krause, K.L. (deposition date: 1998-07-23, release date: 1999-09-10, Last modification date: 2024-05-22)

Primary citation

Tanner, J.J.,Tu, S.C.,Barbour, L.J.,Barnes, C.L.,Krause, K.L.
Unusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase P.
Protein Sci., 8:1725-1732, 1999

PubMed Abstract: 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).

PubMed: 10493573

Experimental method

X-RAY DIFFRACTION (2.08 Å)