Premium
Structures of F 420 H 2 :NADP + oxidoreductase with and without its substrates bound
Author(s) -
Warkentin Eberhard,
Mamat Björn,
SordelKlippert Melanie,
Wicke Michaela,
Thauer Rudolf K.,
Iwata Momi,
Iwata So,
Ermler Ulrich,
Shima Seigo
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.23.6561
Subject(s) - planck , philosophy , art history , chemistry , humanities , physics , art , quantum mechanics
Cofactor F 420 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 F 420 ‐dependent oxidoreductase bound with F 420 . The structure of F 420 H 2 :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.