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Contents 1 Description 1.1 Ferredoxin-NADP+ Reductase 1.2 Activity 2 Structure 3 References

Description

Ferredoxin-NADP+ Reductase

Ferredoxin-NADP+ reductase (FRN), also called ferredoxin-NADP+ oxidoreductase

Activity

Structure

spinqualitylabelsall models PDB ID 1frn Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1frn, resolution 2.00Å ()
Ligands:	, ,
Activity:	Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Structural annotation: Resources: CATH : 1Frn001, 1Frn002 InterPro : Ipr015701, Ipr001709, Ipr001433, Ipr012146 Pfam : PF00175 SCOP : d1frn_2, d1frn_1 UniProt : P00455
Functional annotation: Cellular component: thylakoid chloroplast thylakoid membrane membrane Biological process: photosynthesis transport electron transport Molecular function: NADP binding oxidoreductase activity protein binding ferredoxin-NADP+ reductase activity FAD binding
Evolutionary conservation: Toggle Conservation Colors: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

Ferredoxin-NADP+ reductase of spinach has two structural domains :

• The first domain, at the N-ter of the protein, is an antiparallel beta barrel that contains the binding site for the FAD cofactor ^[1].
• The second domain, at the C-ter of the protein, contains an alpha-helix-beta strand fold ^[1]. This terminal domain is where the NADP+ binds ^[2].

The interface between these two domains is actually the active site of the ferredoxin-NADP+ reductase.

References

1. ↑ ^{1.0 1.1} Aliverti A, Pandini V, Pennati A, de Rosa M, Zanetti G. Structural and functional diversity of ferredoxin-NADP(+) reductases. Arch Biochem Biophys. 2008 Jun 15;474(2):283-91. Epub 2008 Feb 16. PMID:18307973 doi:10.1016/j.abb.2008.02.014
2. ↑ Paladini DH, Musumeci MA, Carrillo N, Ceccarelli EA. Induced fit and equilibrium dynamics for high catalytic efficiency in ferredoxin-NADP(H) reductases. Biochemistry. 2009 Jun 23;48(24):5760-8. PMID:19435322 doi:10.1021/bi9004232