7B2C
Crystal structure of the ethyl-coenzyme M reductase from Candidatus Ethanoperedens thermophilum gassed with xenon
Summary for 7B2C
| Entry DOI | 10.2210/pdb7b2c/pdb |
| Descriptor | Ethyl-Coenzyme M reductase alpha subunit, XENON, CHLORIDE ION, ... (15 entities in total) |
| Functional Keywords | ethyl-com reductase, methyl-com reductase, xenon-derivatization, ethane-oxidizers, f430-cofactor, post-translational modification, gas channel, coenzyme m, coenzyme b, true atomic resolution, thermophile, archaea., transferase |
| Biological source | Candidatus Ethanoperedens thermophilum More |
| Total number of polymer chains | 6 |
| Total formula weight | 300576.59 |
| Authors | Wagner, T.,Lemaire, O.N.,Engilberge, S. (deposition date: 2020-11-26, release date: 2021-07-14, Last modification date: 2024-01-31) |
| Primary citation | Hahn, C.J.,Lemaire, O.N.,Kahnt, J.,Engilberge, S.,Wegener, G.,Wagner, T. Crystal structure of a key enzyme for anaerobic ethane activation. Science, 373:118-121, 2021 Cited by PubMed Abstract: 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 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. PubMed: 34210888DOI: 10.1126/science.abg1765 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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