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-Structure paper
タイトル | De novo modeling of the F(420)-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. |
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ジャーナル・号・ページ | Elife, Vol. 2, Page e00218, Year 2013 |
掲載日 | 2013年3月5日 |
著者 | Deryck J Mills / Stella Vitt / Mike Strauss / Seigo Shima / Janet Vonck / |
PubMed 要旨 | 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 ...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. DOI:http://dx.doi.org/10.7554/eLife.00218.001. |
リンク | Elife / PubMed:23483797 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4 - 4.5 Å |
構造データ | |
化合物 | ChemComp-FCO: ChemComp-NI: ChemComp-FE2: ChemComp-SF4: ChemComp-F42: ChemComp-FAD: |
由来 |
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キーワード | OXIDOREDUCTASE (酸化還元酵素) / METHANOGENESIS (メタン生成経路) |