1go2: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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. | ||
==About this Structure== | ==About this Structure== | ||
1GO2 is a | 1GO2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena Anabaena] with SO4 and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GO2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
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Revision as of 14:17, 5 November 2007
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STRUCTURE OF FERREDOXIN-NADP+ REDUCTASE WITH LYS 72 REPLACED BY GLU (K72E)
OverviewOverview
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.
About this StructureAbout this Structure
1GO2 is a Single protein structure of sequence from Anabaena with SO4 and FAD as ligands. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners., Mayoral T, Martinez-Julvez M, Perez-Dorado I, Sanz-Aparicio J, Gomez-Moreno C, Medina M, Hermoso JA, Proteins. 2005 May 15;59(3):592-602. PMID:15789405
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