Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  DetailsÜbersicht

Freigegeben
Zeitschriftenartikel

De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy

MPG-Autoren
/persons/resource/persons137802

Mills,  Deryck J.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137931

Vitt,  Stella
Max Planck Institute for terrestrial Microbiology, Max Planck Society;

/persons/resource/persons137910

Strauss,  Mike
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

Shima,  Seigo
Max Planck Institute for terrestrial Microbiology, Max Planck Society;
Japan Science and Technology Agency Kawaguchi, Japan;

/persons/resource/persons137933

Vonck,  Janet
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Mills, D. J., Vitt, S., Strauss, M., Shima, S., & Vonck, J. (2013). De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. eLife, 2: e00218. doi:10.7554/eLife.00218.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0024-D509-3
Zusammenfassung
Methanogenic archaea use a [NiFe]-hydrogenase, Frh, for oxidation/reduction of F420, an important hydride carrier in the methanogenesis pathway from H2 and CO2. Frh accounts for about 1% of the cytoplasmic protein and forms a huge complex consisting of FrhABG heterotrimers with each a [NiFe] center, four Fe-S clusters and an FAD. Here, we report the structure determined by near-atomic resolution cryo-EM of Frh with and without bound substrate F420. The polypeptide chains of FrhB, for which there was no homolog, was traced de novo from the EM map. The 1.2-MDa complex contains 12 copies of the heterotrimer, which unexpectedly form a spherical protein shell with a hollow core. The cryo-EM map reveals strong electron density of the chains of metal clusters running parallel to the protein shell, and the F420-binding site is located at the end of the chain near the outside of the spherical structure.