Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound

Warkentin, Eberhard; Mamat, Björn; Sordel-Klippert, Melanie; Wicke, Michaela; Thauer, Rudolf K.; Iwata, Momi; Iwata, So; Ermler, Ulrich; Shima, Seigo

doi:10.1093/emboj/20.23.6561

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Structures of F₄₂₀H²:NADP⁺ oxidoreductase with and without its substrates bound

MPS-Authors

/persons/resource/persons137939

Warkentin, Eberhard
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137790

Mamat, Björn
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Sordel-Klippert, Melanie
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Wicke, Michaela
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254760

Thauer, Rudolf K.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons137648

Ermler, Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons254714

Shima, Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

External Resource

https://doi.org/10.1093/emboj/20.23.6561
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Warkentin, E., Mamat, B., Sordel-Klippert, M., Wicke, M., Thauer, R. K., Iwata, M., et al. (2001). Structures of F₄₂₀H²:NADP⁺ oxidoreductase with and without its substrates bound. The EMBO Journal, 20(23), 6561 -6569. doi:10.1093/emboj/20.23.6561.

Cite as: https://hdl.handle.net/21.11116/0000-0009-4418-0

Abstract

Cofactor F₄₂₀ is a 5′-deazaflavin derivative first discovered in methanogenic archaea but later found also to be present in some bacteria. As a coenzyme, it is involved in hydride transfer reactions and as a prosthetic group in the DNA photolyase reaction. We report here for the first time on the crystal structure of an F₄₂₀-dependent oxidoreductase bound with F₄₂₀. The structure of F₄₂₀H²:NADP⁺ oxidoreductase resolved to 1.65 Å contains two domains: an N-terminal domain characteristic of a dinucleotide-binding Rossmann fold and a smaller C-terminal domain. The nicotinamide and the deazaflavin part of the two coenzymes are bound in the cleft between the domains such that the Si-faces of both face each other at a distance of 3.1 Å, which is optimal for hydride transfer. Comparison of the structures bound with and without substrates reveals that of the two substrates NADP has to bind first, the binding being associated with an induced fit.