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

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.

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 Creators:
Mills, Deryck J.1, Author              
Vitt, Stella2, Author              
Strauss, Mike1, Author              
Shima, Seigo2, 3, Author
Vonck, Janet1, Author              
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Max Planck Institute for terrestrial Microbiology, Max Planck Society, Karl-von-Frisch-Strasse 10, D-35043 Marburg, DE, ou_3135468              
3Japan Science and Technology Agency Kawaguchi, Japan, ou_persistent22              

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Free keywords: Methanothermobacter marburgensis; Other; cryo-electron microscopy; hydrogenase; methanogenesis
 Abstract: 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.

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Language(s): eng - English
 Dates: 2012-09-042013-01-252013-03-05
 Publication Status: Published online
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 634883
DOI: 10.7554/eLife.00218
 Degree: -

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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 2 Sequence Number: e00218 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X