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Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically

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Shima,  Seigo
Max Planck Institute of Biophysics, Max Planck Society;

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Weinert,  Tobias
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Demmer,  Ulrike
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kahnt,  Jörg
Max Planck Institute of Biophysics, Max Planck Society;

Thauer,  Rudolf K.
Max Planck Society;

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Ermler,  Ulrich
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Shima, S., Krueger, M., Weinert, T., Demmer, U., Kahnt, J., Thauer, R. K., et al. (2012). Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically. Nature, 481(7379), 98-101.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-D586-B
Abstract
The anaerobic oxidation of methane (AOM) with sulphate, an area currently generating great interest in microbiology, is accomplished by consortia of methanotrophic archaea (ANME) and sulphatereducing bacteria. The enzyme activating methane in methanotrophic archaea has tentatively been identified as a homologue of methyl-coenzyme M reductase (MCR) that catalyses the methaneforming step in methanogenic archaea. Here we report an X-ray structure of the 280 kDa heterohexameric ANME-1MCRcomplex. It was crystallized uniquely from a protein ensemble purified from consortia of microorganisms collected with a submersible from a Black Sea mat catalysing AOM with sulphate. Crystals grown from the heterogeneous sample diffract to 2.1 Å resolution and consist of a single ANME-1MCR population, demonstrating the strong selective power of crystallization. The structure revealed ANME-1 MCR in complex with coenzyme M and coenzyme B, indicating the same substrates for MCR from methanotrophic and methanogenic archaea. Differences between the highly similar structures of ANME-1MCR and methanogenic MCR include a F430 modification, a cysteine-rich patch and an altered post-translational amino acid modification pattern,whichmaytune the enzymes for their functions in different biological contexts.