title: Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.
abstract: Ferredoxin (Fd) interacts with ferredoxin-NADP(+) reductase (FNR) to transfer two electrons to the latter, one by one, which will finally be used to reduce NADP(+) to NADPH. The formation of a transient complex between Fd and FNR is required for the electron transfer (ET), and extensive mutational and crystallographic studies have been reported to characterize such protein-protein interaction. However, some aspects of the association mechanism still remain unclear. Moreover, in spite of their structural differences, flavodoxin (Fld) can replace Fd in its function and interact with FNR to transfer electrons with only slightly lower efficiency. Although crystallographic structures for the FNR:Fd association have been reported, experimental structural data for the FNR:Fld interaction are highly elusive. We have modeled here the interactions between FNR and both of its protein partners, Fd and Fld, using surface energy analysis, computational rigid-body docking simulations, and interface side-chain refinement. The results, consistent with previous experimental data, suggest the existence of alternative binding modes in these ET proteins.
authors.affiliation: Department of Biochemistry and Molecular and Cellular Biology, University of Zaragoza, Zaragoza, Spain.
authors.forename: Milagros
authors.initials: M
authors.lastname: Medina
authors.forename: Ruben
authors.initials: R
authors.lastname: Abagyan
authors.forename: Carlos
authors.initials: C
authors.lastname: Gómez-Moreno
authors.forename: Juan
authors.initials: J
authors.lastname: Fernandez-Recio
mesh_terms: D000595:Amino Acid Sequence; D017033:Anabaena / Q000201:enzymology*; D004583:Electrons; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry / Q000378:metabolism*; D005288:Ferredoxins / Q000378:metabolism*; D005418:Flavodoxin / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry; D017433:Protein Structure, Secondary
chemical_list: D005288:Ferredoxins; D005418:Flavodoxin; D050505:Mutant Proteins; D005287:Ferredoxin-NADP Reductase; D008239:Lysine