NDLI: Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Medina, Milagros Abagyan, Ruben Gómez-Moreno, Carlos Fernandez-Recio, Juan
Description	Country affiliation: Spain Author Affiliation: Medina M ( Department of Biochemistry and Molecular and Cellular Biology, University of Zaragoza, Zaragoza, Spain.)
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.
File Format	HTM / HTML
ISSN	08873585
e-ISSN	10970134
DOI	10.1002/prot.21979
Journal	Proteins: Structure, Function, and Bioinformatics
Issue Number	3
Volume Number	72
Language	English
Publisher	Wiley-Liss
Publisher Date	2008-08-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acid Sequence Research Support, Non-u.s. Gov't Protein Structure, Secondary Discipline Biochemistry Models, Molecular Molecular Sequence Data Metabolism Mutagenesis, Site-directed Mutant Proteins Chemistry Lysine Ferredoxin-nadp Reductase Anabaena Ferredoxins Flavodoxin Enzymology Electrons
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry Molecular Biology

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Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NADP+ reductase: site-specific mutagenesis, transient kinetic measurements, and electrostatic surface potentials.

Docking Analysis of Transient Complexes: Interaction of Ferredoxin-NADP+ Reductase with Ferredoxin and Flavodoxin

External loops at the $ferredoxin-NADP^{+}$ reductase protein–partner binding cavity contribute to substrates allocation

A hydrogen bond network in the active site of Anabaena $ferredoxin-NADP^{+}$ reductase modulates its catalytic efficiency

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Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.

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