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Docking analysis of transient complexes: Interaction of ferredoxin‐NADP+ reductase with ferredoxin and flavodoxin

Proteins Structure Function and Bioinformatics2008Vol. 72(3), pp. 848–862

Citations Over TimeTop 18% of 2008 papers

Milagros Medina, Ruben Abagyan, Carlos Gómez‐Moreno, Juan Fernández‐Recio

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.

Citations Over TimeTop 18% of 2008 papers

Abstract

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