Publication Date:
2011-11-29
Description:
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 A 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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shima, Seigo -- Krueger, Martin -- Weinert, Tobias -- Demmer, Ulrike -- Kahnt, Jorg -- Thauer, Rudolf K -- Ermler, Ulrich -- England -- Nature. 2011 Nov 27;481(7379):98-101. doi: 10.1038/nature10663.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Terrestrial Microbiology, Karl-Frisch-Strasse 10, D-35043 Marburg, Germany. shima@mpi-marburg.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22121022" target="_blank"〉PubMed〈/a〉
Keywords:
Anaerobiosis
;
Archaea/*enzymology/isolation & purification/metabolism
;
*Biocatalysis
;
Black Sea
;
Catalytic Domain
;
Coenzymes/chemistry/metabolism
;
Crystallography, X-Ray
;
Cysteine/metabolism
;
Expeditions
;
Methane/*metabolism
;
Models, Molecular
;
Oxidation-Reduction
;
Oxidoreductases/*chemistry/*metabolism
;
Protein Conformation
;
Seawater/*microbiology
;
Ships
;
Sulfates/metabolism
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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