spacer Cryo-EM structure of the F420-reducing NiFe-hydrogenase from a methanogenic archaeon with bound substrate
Primary citation
Title De Novo Modeling of the F420-Reducing [Nife]-Hydrogenase from a Methanogenic Archaeon by Cryo-Electron Microscopy
Authors Mills, D.J.search; Vitt, S.search; Strauss, M.search; Shima, S.search; Vonck, J.search
Journal ELIFEsearch vol:2, pag:218 (2013), Identifiers: PubMed ID (23483797)search DOI (10.7554/eLife.00218)
Abstract 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.
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