7b2h | pdb_00007b2h

Crystal structure of the methyl-coenzyme M reductase from Methanothermobacter Marburgensis derivatized with xenon

spinqualitylabelsall models 7b2h, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b2h is a 6 chain structure with sequence from Methanothermobacter marburgensis str. Marburg. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.12Å Ligands: AGM, CL, COM, DYA, EDO, F43, GL3, GOL, K, MG, MGN, MHS, PEG, SMC, SO4, TP7, XE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MCRA_METTM Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. Publication Abstract from PubMed Ethane, the second most abundant hydrocarbon gas in the seafloor, is efficiently oxidized by anaerobic archaea in syntrophy with sulfate-reducing bacteria. Here, we report the 0.99-angstrom-resolution structure of the proposed ethane-activating enzyme and describe the specific traits that distinguish it from methane-generating and -consuming methyl-coenzyme M reductases. The widened catalytic chamber, harboring a dimethylated nickel-containing F(430) cofactor, would adapt the chemistry of methyl-coenzyme M reductases for a two-carbon substrate. A sulfur from methionine replaces the oxygen from a canonical glutamine as the nickel lower-axial ligand, a feature conserved in thermophilic ethanotrophs. Specific loop extensions, a four-helix bundle dilatation, and posttranslational methylations result in the formation of a 33-angstrom-long hydrophobic tunnel, which guides the ethane to the buried active site as confirmed with xenon pressurization experiments. Crystal structure of a key enzyme for anaerobic ethane activation.,Hahn CJ, Lemaire ON, Kahnt J, Engilberge S, Wegener G, Wagner T Science. 2021 Jul 2;373(6550):118-121. doi: 10.1126/science.abg1765. PMID:34210888 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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