Structural highlights
Function[F42NO_ARCFU] Catalyzes the reversible reduction of NADP(+) by F420H(2). In this reaction the proS hydrogen at C5 of F420 is transferred into the proS position at C4 of NADPH. Has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCofactor 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 A 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 A, 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. Structures of F420H2:NADP+ oxidoreductase with and without its substrates bound.,Warkentin E, Mamat B, Sordel-Klippert M, Wicke M, Thauer RK, Iwata M, Iwata S, Ermler U, Shima S EMBO J. 2001 Dec 3;20(23):6561-9. PMID:11726492[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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