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Ferredoxin-NADP+ reductase of spinach is made of two structural domains :
Ferredoxin-NADP+ reductase of spinach is made of two structural domains :
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*The first domain, from the residue 20 to 162 at the N-ter of the protein, is a six-stranded antiparallel β-barrel with a peripheral two-stranded antiparallel hairpin and a final α-helix of eight residues <ref name=Karplus2>doi:10.1007/BF00763221</ref> . This domain contain the binding site for the FAD cofactor <ref name=Aliverti>doi:10.1016/j.abb.2008.02.014</ref> which binds its adenosine-diphosphate part to the hairpin and helix <ref name=Karplus2>doi:10.1007/BF00763221</ref>.
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*The first domain, from the residue 20 to 162 at the N-ter of the protein, is a six-stranded antiparallel β-barrel with a peripheral two-stranded antiparallel hairpin and a final α-helix of eight residues <ref name=Karplus2>PMID:8027025</ref> . This domain contain the binding site for the FAD cofactor <ref name=Aliverti>doi:10.1016/j.abb.2008.02.014</ref> which binds its adenosine-diphosphate part to the hairpin and helix <ref name=Karplus2>doi:10.1007/BF00763221</ref>.
*The second domain, at the C-ter of the protein, contains an alpha-helix-beta strand fold <ref name=Aliverti>doi:10.1016/j.abb.2008.02.014</ref>. This terminal domain is where the NADP+ binds <ref name=Paladini>doi:10.1021/bi9004232</ref>.
*The second domain, at the C-ter of the protein, contains an alpha-helix-beta strand fold <ref name=Aliverti>doi:10.1016/j.abb.2008.02.014</ref>. This terminal domain is where the NADP+ binds <ref name=Paladini>doi:10.1021/bi9004232</ref>.

Revision as of 01:05, 30 December 2011

Contents

Description

Enzyme

Ferredoxin-NADP+ reductase (FRN), also called ferredoxin-NADP+ oxidoreductase, is a flavoprotein which can be mainly found in chloroplasts, mitochondria and bacteria. This enzyme is a member of the family of oxidoreductases, that use iron-sulfur proteins as electron donors and NAD+ or NADP+ as electron acceptors. In plants, this is an ubiquitous hydrophilic protein of about 35 kDa which 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 catalyzes the electron transfer between the electron carrier protein ferredoxin (Fd) and NADP(H).

Ferredoxin-NADP+ reductase owns three different substrates :

  • reduced ferredoxin
  • NADP+
  • H+

This protein also have 2 cofactors :

  • FAD
  • Flavin

Activity

Structure

PDB ID 1frn

Drag the structure with the mouse to rotate
1frn, resolution 2.00Å ()
Ligands: , ,
Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


General 3D structure description

Structural informations of ferredoxin-NADP+ reductase has been found by crystallography. The most recent crystal structure was reported in the literature at 1.7Å resolution [1].

Ferredoxin-NADP+ reductase of spinach is made of two structural domains :

  • The first domain, from the residue 20 to 162 at the N-ter of the protein, is a six-stranded antiparallel β-barrel with a peripheral two-stranded antiparallel hairpin and a final α-helix of eight residues [2] . This domain contain the binding site for the FAD cofactor [3] which binds its adenosine-diphosphate part to the hairpin and helix [2].
  • The second domain, at the C-ter of the protein, contains an alpha-helix-beta strand fold [3]. This terminal domain is where the NADP+ binds [4].

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

Important residues for structure

Residues involved in binding of substrates and cofactors

NADP binding

Ferredoxin binding

FAD binding

References

  1. ↑ Bruns CM, Karplus PA. Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound states. J Mol Biol. 1995 Mar 17;247(1):125-45. PMID:7897656
  2. ↑ 2.0 2.1 Karplus PA, Bruns CM. Structure-function relations for ferredoxin reductase. J Bioenerg Biomembr. 1994 Feb;26(1):89-99. PMID:8027025
  3. ↑ 3.0 3.1 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
  4. ↑ 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

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Yoann Styczen

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