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*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>. | ||
| - | The | + | The interface between these two domains is actually the active site of the ferredoxin NADP+ reductase. |
== References == | == References == | ||
<references /> | <references /> | ||
Revision as of 17:19, 28 December 2011
Contents |
Description
Ferredoxin NADP+ Reductase
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 | ||||||||
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
- ↑ 1.0 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
