3sqg

Crystal structure of a methyl-coenzyme M reductase purified from Black Sea mats

spinqualitylabelsall models 3sqg, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3sqg is a 9 chain structure with sequence from Uncultured archaeon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: 0AF, 1PE, CA, CL, COM, GL3, GOL, M43, MHO, MHS, P6G, PGE, SO4, TP7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D1JBK4_UNCAX Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.[PIRNR:PIRNR000262] Publication Abstract from PubMed 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. Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically.,Shima S, Krueger M, Weinert T, Demmer U, Kahnt J, Thauer RK, Ermler U Nature. 2011 Nov 27. doi: 10.1038/nature10663. PMID:22121022 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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