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PDBsum entry 1go2
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Oxidoreductase
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PDB id
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1go2
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural analysis of interactions for complex formation between ferredoxin-Nadp+ reductase and its protein partners.
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Authors
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T.Mayoral,
M.Martínez-Júlvez,
I.Pérez-Dorado,
J.Sanz-Aparicio,
C.Gómez-Moreno,
M.Medina,
J.A.Hermoso.
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Ref.
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Proteins, 2005,
59,
592-602.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
59,
592-602)
copyright 2005.
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Secondary reference #1
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Title
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X-Ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium anabaena pcc 7119 at 1.8 a resolution, And crystallographic studies of NADP+ binding at 2.25 a resolution.
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Authors
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L.Serre,
F.M.Vellieux,
M.Medina,
C.Gomez-Moreno,
J.C.Fontecilla-Camps,
M.Frey.
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Ref.
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J Mol Biol, 1996,
263,
20-39.
[DOI no: ]
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PubMed id
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Figure 5.
Figure 5. Interaction between FNR and ferredoxin. The charged residues, which are probably involved in the binding
of FNR with ferredoxin and are currently mutated, are represented by thick lines.
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Figure 8.
Figure 8. A stereoscopic view of the difference electron density at the NADP
+
site (contoured at 2s) calculated with
phases from a model obtained by refining the native FNR X-ray model at 1.8 Å resolution (omitting residue 1 to 8,
the sulfate ion and the water molecules) by simulated annealing and energy minimization against the amplitudes from
the FNR-NADP
+
crystal. The final NADP
+
position is represented.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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