spacer
spacer

PDBsum entry 1qgy

Go to PDB code: 
protein ligands links
Oxidoreductase PDB id
1qgy
Jmol
Contents
Protein chain
295 a.a. *
Ligands
SO4
FAD
Waters ×500
* Residue conservation analysis
PDB id:
1qgy
Name: Oxidoreductase
Title: Ferredoxin:nadp+ reductase mutant with lys 75 replaced by gl
Structure: Ferredoxin--NADP+ reductase. Chain: a. Synonym: fnr. Engineered: yes. Mutation: yes
Source: Nostoc sp.. Organism_taxid: 1168. Strain: pcc 7119. Gene: peth. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.200     R-free:   0.230
Authors: J.A.Hermoso,T.Mayoral,M.Medina,M.Martinez-Ripoll,M.Martinez- J.Sanz-Aparicio,C.Gomez-Moreno
Key ref:
T.Mayoral et al. (2005). Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners. Proteins, 59, 592-602. PubMed id: 15789405 DOI: 10.1002/prot.20450
Date:
10-May-99     Release date:   09-Mar-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P21890  (FENR_ANASO) -  Ferredoxin--NADP reductase
Seq:
Struc:
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.1.18.1.2  - Ferredoxin--NADP(+) reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Methionine Synthase
      Reaction: 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
2 × reduced ferredoxin
+ NADP(+)
+ H(+)
= 2 × oxidized ferredoxin
+ NADPH
      Cofactor: FAD
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  

 

 
    reference    
 
 
DOI no: 10.1002/prot.20450 Proteins 59:592-602 (2005)
PubMed id: 15789405  
 
 
Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners.
T.Mayoral, M.Martínez-Júlvez, I.Pérez-Dorado, J.Sanz-Aparicio, C.Gómez-Moreno, M.Medina, J.A.Hermoso.
 
  ABSTRACT  
 
The three-dimensional structures of K72E, K75R, K75S, K75Q, and K75E Anabaena Ferredoxin-NADP+ reductase (FNR) mutants have been solved, and particular structural details of these mutants have been used to assess the role played by residues 72 and 75 in optimal complex formation and electron transfer (ET) between FNR and its protein redox partners Ferredoxin (Fd) and Flavodoxin (Fld). Additionally, because there is no structural information available on the interaction between FNR and Fld, a model for the FNR:Fld complex has also been produced based on the previously reported crystal structures and on that of the rat Cytochrome P450 reductase (CPR), onto which FNR and Fld have been structurally aligned, and those reported for the Anabaena and maize FNR:Fd complexes. The model suggests putative electrostatic and hydrophobic interactions between residues on the FNR and Fld surfaces at the complex interface and provides an adequate orientation and distance between the FAD and FMN redox centers for efficient ET without the presence of any other molecule as electron carrier. Thus, the models now available for the FNR:Fd and FNR:Fld interactions and the structures presented here for the mutants at K72 and K75 in Anabaena FNR have been evaluated in light of previous biochemical data. These structures confirm the key participation of residue K75 and K72 in complex formation with both Fd and Fld. The drastic effect in FNR activity produced by replacement of K75 by Glu in the K75E FNR variant is explained not only by the observed changes in the charge distribution on the surface of the K75E FNR mutant, but also by the formation of a salt bridge interaction between E75 and K72 that simultaneously "neutralizes" two essential positive charged side chains for Fld/Fd recognition.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Molecular surface showing the electrostatic potentials of (A) WT FNR and (B) WT Fld. Positive charges are shown in blue and negative ones in red. The FAD and FMN cofactors are represented as sticks.
Figure 5.
Figure 5. (A) Putative FNR:Fld complex showing the relative position of FAD and FMN cofactors, (B) charged residues at the FNR:Fld interface. (C) Hydrophobic residues on FNR and Fld in the putative complex. In all representations, Fld is colored in yellow and FNR in blue. (D) Crystal structure of FNR:Fd complex (PDB code 1EWY) showing the relative position of the redox centers. (E) Charged residues at the FNR:Fd interface. (F) Hydrophobic residues on FNR and Fd in the crystal structure of the complex.
 
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 59, 592-602) copyright 2005.  
  Figures were selected by the author.  

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.  
19846550 M.Winkler, S.Kuhlgert, M.Hippler, and T.Happe (2009).
Characterization of the key step for light-driven hydrogen evolution in green algae.
  J Biol Chem, 284, 36620-36627.  
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.  
16766617 A.Velazquez-Campoy, G.Goñi, J.R.Peregrina, and M.Medina (2006).
Exact analysis of heterotropic interactions in proteins: Characterization of cooperative ligand binding by isothermal titration calorimetry.
  Biophys J, 91, 1887-1904.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.