PDBsum entry 1bjk

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Oxidoreductase PDB id
Protein chain
295 a.a. *
Waters ×332
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Ferredoxin:nadp+ reductase mutant with arg 264 replaced by g
Structure: Ferredoxin--NADP+ reductase. Chain: a. Synonym: fnr. Engineered: yes. Mutation: yes
Source: Nostoc sp.. Organism_taxid: 1168. Strain: pcc 7119. Expressed in: escherichia coli. Expression_system_taxid: 562
2.30Å     R-factor:   0.166     R-free:   0.224
Authors: J.A.Hermoso,T.Mayoral,M.Medina,M.Martinez-Ripoll,M.Martinez- J.Sanz-Aparicio,C.Gomez-Moreno
Key ref:
M.Martínez-Júlvez et al. (1998). Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer. Biochemistry, 37, 17680-17691. PubMed id: 9922134 DOI: 10.1021/bi981718i
25-Jun-98     Release date:   04-Nov-98    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P21890  (FENR_ANASO) -  Ferredoxin--NADP reductase
440 a.a.
295 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Ferredoxin--NADP(+) reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

Methionine Synthase
      Reaction: 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
2 × reduced ferredoxin
+ NADP(+)
+ H(+)
= 2 × oxidized ferredoxin
      Cofactor: FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity     1 term  


DOI no: 10.1021/bi981718i Biochemistry 37:17680-17691 (1998)
PubMed id: 9922134  
Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer.
M.Martínez-Júlvez, J.Hermoso, J.K.Hurley, T.Mayoral, J.Sanz-Aparicio, G.Tollin, C.Gómez-Moreno, M.Medina.
Previous studies and the crystal structure of Anabaena PCC 7119 FNR suggest that the side chains of Arg100 and Arg264 may be directly involved in the proper NADP+/NADPH orientation for an efficient electron-transfer reaction. Protein engineering on Arg100 and Arg264 from Anabaena PCC 7119 FNR has been carried out to investigate their roles in complex formation and electron transfer to NADP+ and to ferredoxin/flavodoxin. Arg100 has been replaced with an alanine, which removes the positive charge, the long side chain, as well as the ability to form hydrogen bonds, while a charge reversal mutation has been made at Arg264 by replacing it with a glutamic acid. Results with various spectroscopic techniques indicate that the mutated proteins folded properly and that significant protein structural rearrangements did not occur. Both mutants have been kinetically characterized by steady-state as well as fast transient kinetic techniques, and the three-dimensional structure of Arg264Glu FNR has been solved. The results reported herein reveal important conceptual information about the interaction of FNR with its substrates. A critical role is confirmed for the long, positively charged side chain of Arg100. Studies on the Arg264Glu FNR mutant demonstrate that the Arg264 side chain is not critical for the nicotinamide orientation or for nicotinamide interaction with the isoalloxazine FAD moiety. However, this mutant showed altered behavior in its interaction and electron transfer with its protein partners, ferredoxin and flavodoxin.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19527656 M.Martínez-Júlvez, M.Medina, and A.Velázquez-Campoy (2009).
Binding thermodynamics of ferredoxin:NADP+ reductase: two different protein substrates and one energetics.
  Biophys J, 96, 4966-4975.  
19583765 M.Medina (2009).
Structural and mechanistic aspects of flavoproteins: photosynthetic electron transfer from photosystem I to NADP+.
  FEBS J, 276, 3942-3958.  
18260112 M.Medina, R.Abagyan, C.Gómez-Moreno, and J.Fernandez-Recio (2008).
Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.
  Proteins, 72, 848-862.  
18658149 S.L.Tu, H.C.Chen, and L.W.Ku (2008).
Mechanistic Studies of the Phytochromobilin Synthase HY2 from Arabidopsis.
  J Biol Chem, 283, 27555-27564.  
16327013 S.L.Tu, W.Sughrue, R.D.Britt, and J.C.Lagarias (2006).
A conserved histidine-aspartate pair is required for exovinyl reduction of biliverdin by a cyanobacterial phycocyanobilin:ferredoxin oxidoreductase.
  J Biol Chem, 281, 3127-3136.  
15789405 T.Mayoral, M.Martínez-Júlvez, I.Pérez-Dorado, J.Sanz-Aparicio, C.Gómez-Moreno, M.Medina, and J.A.Hermoso (2005).
Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners.
  Proteins, 59, 592-602.
PDB codes: 1e62 1e63 1e64 1go2 1qgy
12581212 M.Faro, B.Schiffler, A.Heinz, I.Nogués, M.Medina, R.Bernhardt, and C.Gómez-Moreno (2003).
Insights into the design of a hybrid system between Anabaena ferredoxin-NADP+ reductase and bovine adrenodoxin.
  Eur J Biochem, 270, 726-735.  
12709048 N.Carrillo, and E.A.Ceccarelli (2003).
Open questions in ferredoxin-NADP+ reductase catalytic mechanism.
  Eur J Biochem, 270, 1900-1915.  
12383252 M.Faro, S.Frago, T.Mayoral, J.A.Hermoso, J.Sanz-Aparicio, C.Gómez-Moreno, and M.Medina (2002).
Probing the role of glutamic acid 139 of Anabaena ferredoxin-NADP+ reductase in the interaction with substrates.
  Eur J Biochem, 269, 4938-4947.
PDB code: 1gr1
10651039 T.Mayoral, M.Medina, J.Sanz-Aparicio, C.Gómez-Moreno, and J.A.Hermoso (2000).
Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119 ferredoxin-NADP+ reductase revealed by x-ray crystallography.
  Proteins, 38, 60-69.
PDB code: 1b2r
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