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

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.

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 Creators:
Warkentin, Eberhard1, Author           
Mamat, Björn1, 2, Author           
Sordel-Klippert, Melanie2, Author
Wicke, Michaela2, Author
Thauer, Rudolf K.2, Author
Iwata, Momi3, Author
Iwata, So3, Author
Ermler, Ulrich1, Author           
Shima, Seigo2, Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, 35043 Marburg, Germany, ou_persistent22              
3Department of Biological Sciences and Division of Biomedical Sciences, Imperial College of Science, Technology and Medicine, London SW7 2AZ, UK, ou_persistent22              

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Free keywords: rystal structure; rug design; F420; hydride transfer; oxidoreductase
 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.

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Language(s): eng - English
 Dates: 2001-10-022001-07-182001-10-182001-12-03
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1093/emboj/20.23.6561
PMID: 11726492
 Degree: -

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Title: The EMBO Journal
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 20 (23) Sequence Number: - Start / End Page: 6561 - 6569 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061_1