3SQG
Crystal structure of a methyl-coenzyme M reductase purified from Black Sea mats
Summary for 3SQG
| Entry DOI | 10.2210/pdb3sqg/pdb |
| Related | 1HBN 3M1V 3POT |
| Descriptor | Methyl coenzyme M reductase, alpha subunit, CHLORIDE ION, CALCIUM ION, ... (14 entities in total) |
| Functional Keywords | anaerobic methane oxidation, transferase |
| Biological source | uncultured archaeon More |
| Total number of polymer chains | 9 |
| Total formula weight | 432501.57 |
| Authors | Shima, S.,Krueger, M.,Weinert, T.,Demmer, U.,Thauer, R.K.,Ermler, U. (deposition date: 2011-07-05, release date: 2011-11-30, Last modification date: 2025-03-26) |
| Primary citation | Shima, S.,Krueger, M.,Weinert, T.,Demmer, U.,Kahnt, J.,Thauer, R.K.,Ermler, U. Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically. Nature, 481:98-101, 2011 Cited by PubMed 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. PubMed: 22121022DOI: 10.1038/nature10663 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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