Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically.
Nature
; 481(7379): 98-101, 2011 Nov 27.
Article
em En
| MEDLINE
| ID: mdl-22121022
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 sulphate-reducing bacteria. The enzyme activating methane in methanotrophic archaea has tentatively been identified as a homologue of methyl-coenzyme M reductase (MCR) that catalyses the methane-forming step in methanogenic archaea. Here we report an X-ray structure of the 280 kDa heterohexameric ANME-1 MCR complex. 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-1 MCR 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-1 MCR and methanogenic MCR include a F(430) modification, a cysteine-rich patch and an altered post-translational amino acid modification pattern, which may tune the enzymes for their functions in different biological contexts.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
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Água do Mar
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Archaea
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Biocatálise
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Metano
Idioma:
En
Revista:
Nature
Ano de publicação:
2011
Tipo de documento:
Article
País de afiliação:
Alemanha