Structural highlights
Function
D9PYF9_METTM
Publication Abstract from PubMed
Methanogenic archaea use a [NiFe]-hydrogenase, Frh, for oxidation/reduction of F, an important hydride carrier in the methanogenesis pathway from H and CO. 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 F. 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 F-binding site is located at the end of the chain near the outside of the spherical structure. http://dx.doi.org/10.7554/eLife.00218.001.
De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy.,Mills DJ, Vitt S, Strauss M, Shima S, Vonck J Elife. 2013;2:e00218. doi: 10.7554/eLife.00218. Epub 2013 Mar 5. PMID:23483797[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mills DJ, Vitt S, Strauss M, Shima S, Vonck J. De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. Elife. 2013;2:e00218. doi: 10.7554/eLife.00218. Epub 2013 Mar 5. PMID:23483797 doi:http://dx.doi.org/10.7554/eLife.00218
