title: Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking.
abstract: Ferredoxin (Fd) and ferredoxin-NADP(+)-reductase (FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance (NMR)-restrained-docking approach, two alternative structural models of the Fd-FNR complex in the presence of NADP+ are proposed. The protein docking simulations were performed with the software BiGGER. NMR titration revealed a 1:1 stoichiometry for the complex and allowed the mapping of the interacting residues at the surface of Fd. The NMR chemical shifts were encoded into distance constraints and used with theoretically calculated electronic coupling between the redox cofactors to propose experimentally validated docked complexes.
authors.affiliation: REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2859-516 Caparica, Portugal.
authors.forename: P Nuno
authors.initials: PN
authors.lastname: Palma
authors.forename: Bernard
authors.initials: B
authors.lastname: Lagoutte
authors.forename: Ludwig
authors.initials: L
authors.lastname: Krippahl
authors.forename: José J G
authors.initials: JJ
authors.lastname: Moura
authors.forename: Françoise
authors.initials: F
authors.lastname: Guerlesquin
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry* / Q000235:genetics; D005288:Ferredoxins / Q000737:chemistry* / Q000235:genetics; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009249:NADP / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D016415:Sequence Alignment; D046939:Synechocystis / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D005288:Ferredoxins; D046911:Macromolecular Substances; D009249:NADP; D005287:Ferredoxin-NADP Reductase