User:Yoann Styczen/Sandbox 203
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{{STRUCTURE_1frn| PDB=1frn | SCENE= }} | {{STRUCTURE_1frn| PDB=1frn | SCENE= }} | ||
=== General 3D structure description === | === 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. | ||
Ferredoxin-NADP+ reductase of spinach has two structural domains : | 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 <ref name=Aliverti>doi:10.1016/j.abb.2008.02.014</ref>. | *The first domain, at the N-ter of the protein, is an antiparallel beta barrel that contains the binding site for the FAD cofactor <ref name=Aliverti>doi:10.1016/j.abb.2008.02.014</ref>. | ||
Revision as of 00:44, 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
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| 1frn, resolution 2.00Å () | |||||||||
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| Ligands: | , , | ||||||||
| Activity: | Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 | ||||||||
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| 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. 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.
Important residues for structure
Residues involved in binding of substrates and cofactors
NADP binding
Ferredoxin binding
FAD binding
References
- ↑ 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
- ↑ 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
