User:Yoann Styczen/Sandbox 203

From Proteopedia

proteopedia linkproteopedia link

Contents 1 Description 1.1 Enzyme 1.2 Activity 2 Structure 3 References

Description

Enzyme

Ferredoxin-NADP+ reductase (FRN), also called ferredoxin-NADP+ oxidoreductase, is a flavoprotein which can be mainly found in chloroplasts, mitochondria and bacteria. In plants, this cellular component is an hydrophilic protein of about 35 kDa and binds to the stromal surface of the thylakoid membrane.

This protein is involved in the last step of the photosynthetic electron transport chain. Indeed, ferredoxin-NADP+ reductase is an enzyme that catalyzes the electron transfer between the electron carrier protein ferredoxin (Fd) and NADP(H).

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