Ferredoxin NADP(+) Oxidoreductase (FNR)

FNR catalyzes the final step of electron transfer to create NADPH in photosynthesis. This structural work was conducted in the laboratory of Dr. P. Andrew Karplus.

This image shows a model of how NADP might bind to FNR to permit hydride transfer between the nicotinamide group of NADP and the isoalloxazine ring of FAD.

Atomic coordinates and experimental diffraction data

The following links connect to the Brookhaven Protein Data Bank, which maintains and distributes the coordinates and data.

• 1FNB: Coordinates of native spinach FNR at 1.7 Å resolution.
• 1FND: Coordinates of spinach FNR bound to the inhibitor 2',5'-ADP, an NADP fragment, at 1.7 Å resolution.
• 1FNC: Coordinates of chemically reduced spinach FNR at 1.7 Å resolution.
• 1FRN: Coordinates and structure factors of spinach FNR with active site residue Ser96 mutated to Val at 2.0 Å resolution.

Related structures determined by other researchers:

Other NADP/NADPH utilizing enzymes

• 1QUE: Coordinates of Anabaena FNR at 1.8 Å resolution.
• 1QUF: Coordinates of Anabaena FNR bound to NADP at 2.25 Å resolution.
• 1FDR: Coordinates of E. coli flavodoxin reductase R126Q mutant at 1.70 Å resolution.
• 1A8P: Coordinates of Azotobacter vinelandii ferredoxin reductase at 2.00 Å resolution.
• 1AMO: Coordinates of rat cytochrome p450 reductase at 2.60 Å resolution.

NAD/NADH utilizing enzymes

• 2PIA: Coordinates of Pseudomonas cepacia phthalate dioxygenase reductase at 2.0 Å resolution.
• 2CND: Coordinates of Corn (Zea mays) nitrate reductase at 2.5 Å resolution.
• 2CNF: Coordinates of Corn (Zea mays) nitrate reductase bound to ADP at 2.7 Å resolution.
• 2CNE: Coordinates of Corn (Zea mays) nitrate reductase C242S mutant at 3.0 Å resolution.
• 1NDH: Coordinates of Pig (Sus scrofa) cytochrome b5 reductase at 2.1 Å resolution.

References

A. Aliverti, C.M. Bruns, V. E. Pandini, P. A. Karplus, M. A. Vanoni, B. Curti, and G. Zanetti (1995) Involvement of Serine 96 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase: Structure-Function Relationship as Studied by Site-Directed Mutagenesis and X-ray Crystallography. Biochemistry 34(26): 8371-8379

C.M. Bruns and P.A. Karplus (1995) Refined Crystal Structure of Spinach Ferredoxin-NADP+ Reductase at 1.7Å Resolution: Oxidized, Reduced, and 2'-phospho-5'-AMP Bound States. Journal of Molecular Biology 247(1): 125-145

P.A. Karplus and C.M. Bruns (1994) Structure Function Relations for Ferredoxin Reductase. J. Bioenerg. Biomembr. 26(1): 89-99

C.M. Bruns and P.A. Karplus (1994) Refined Structures of Native, Complexed, and Reduced Forms of Spinach Ferredoxin Reductase. In: Flavins and Flavoproteins 1993 Ed.: K. Yagi., Walter de Gruyter and Co., Berlin pp. 443-445

C.C. Correll, M.L. Ludwig, C.M. Bruns, and P.A. Karplus (1993) Structural Prototypes for an Extended Family of Flavoprotein Reductases: Comparison of Phthalate Dioxygenase Reductase with Ferredoxin Reductase and Ferredoxin. Protein Science 2(12): 2112-2133

C.M. Bruns and P.A. Karplus (1993) Sequence/structure Relationships in Enzymes Related to Ferredoxin Reductase. Presented at the 3rd annual Beckman Institute Symposium on Protein Structure and Function, Urbana/Champaign, Illinois, June 3-6, 1993

C.M. Bruns and P.A. Karplus (1992) Refined Crystal Structure of Spinach Ferredoxin Reductase at 1.7Å Resolution. Presented at the 1992 meeting of the American Crystallographic Association (ACA), University of Pittsburgh, Pittsburgh, PA, July, 1992

P.A. Karplus, M.J. Daniels, and J.R. Herriott (1991) Atomic Structure of Ferredoxin-NADP+ Reductase: Prototype for a Structurally Novel Flavoenzyme Family. Science 251: 60-66

C.M. Bruns and P.A. Karplus (1991) Evaluation of Secondary Structure Predictions for Enzymes Related to Ferredoxin Reductase. In: Flavins and Flavoproteins 1990 Eds.: B. Curti, S. Ronchi, and G. Zanetti. Walter de Gruyter and Co., Berlin pp. 487-490

FNR related links

• Structural studies of ferredoxin:NADP+ reductase family

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