De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy
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,...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2013-03-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/00218 |
| _version_ | 1811201233596186624 |
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| author | Deryck J Mills Stella Vitt Mike Strauss Seigo Shima Janet Vonck |
| author_facet | Deryck J Mills Stella Vitt Mike Strauss Seigo Shima Janet Vonck |
| author_sort | Deryck J Mills |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-12T02:17:34Z |
| format | Article |
| id | doaj.art-22294937e4b147abb9ab57dffd3c9c31 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T02:17:34Z |
| publishDate | 2013-03-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-22294937e4b147abb9ab57dffd3c9c312022-12-22T03:52:12ZengeLife Sciences Publications LtdeLife2050-084X2013-03-01210.7554/eLife.00218De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopyDeryck J Mills0Stella Vitt1Mike Strauss2Seigo Shima3Janet Vonck4Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, GermanyMax Planck Institute for Terrestrial Microbiology, Marburg, GermanyDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, GermanyMax Planck Institute for Terrestrial Microbiology, Marburg, Germany; PRESTO, Japan Science and Technology Agency, Kawaguchi, JapanDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, GermanyMethanogenic 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.https://elifesciences.org/articles/00218Methanothermobacter marburgensiscryo-electron microscopymethanogenesishydrogenase |
| spellingShingle | Deryck J Mills Stella Vitt Mike Strauss Seigo Shima Janet Vonck De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy eLife Methanothermobacter marburgensis cryo-electron microscopy methanogenesis hydrogenase |
| title | De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy |
| title_full | De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy |
| title_fullStr | De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy |
| title_full_unstemmed | De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy |
| title_short | De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy |
| title_sort | de novo modeling of the f420 reducing nife hydrogenase from a methanogenic archaeon by cryo electron microscopy |
| topic | Methanothermobacter marburgensis cryo-electron microscopy methanogenesis hydrogenase |
| url | https://elifesciences.org/articles/00218 |
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