7NKG
Methyl-coenzyme M reductase from Methermicoccus shengliensis at 1.6-A resolution
Summary for 7NKG
| Entry DOI | 10.2210/pdb7nkg/pdb |
| Descriptor | Methyl-coenzyme M reductase alpha subunit, Methyl-coenzyme M reductase beta subunit, Methyl-coenzyme M reductase gamma subunit, ... (10 entities in total) |
| Functional Keywords | methyl-coenzyme m reductase, cofactor f430, post-translational modification, archaea, methoxydotrophy, methanogenesis, coenzyme m, coenzyme b, heterodisulfide, radical mechanism, thermophile, thioglycine, transferase |
| Biological source | Methermicoccus shengliensis DSM 18856 More |
| Total number of polymer chains | 12 |
| Total formula weight | 551715.60 |
| Authors | Mueller, M.,Wagner, T. (deposition date: 2021-02-18, release date: 2021-05-19, Last modification date: 2024-01-31) |
| Primary citation | Kurth, J.M.,Muller, M.C.,Welte, C.U.,Wagner, T. Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications. Microorganisms, 9:-, 2021 Cited by PubMed Abstract: Methanogenic archaea operate an ancient, if not primordial, metabolic pathway that releases methane as an end-product. This last step is orchestrated by the methyl-coenzyme M reductase (MCR), which uses a nickel-containing F-cofactor as the catalyst. MCR astounds the scientific world by its unique reaction chemistry, its numerous post-translational modifications, and its importance in biotechnology not only for production but also for capturing the greenhouse gas methane. In this report, we investigated MCR natively isolated from . This methanogen was isolated from a high-temperature oil reservoir and has recently been shown to convert lignin and coal derivatives into methane through a process called methoxydotrophic methanogenesis. A methoxydotrophic culture was obtained by growing with 3,4,5-trimethoxybenzoate as the main carbon and energy source. Under these conditions, MCR represents more than 12% of the total protein content. The native MCR structure refined at a resolution of 1.6-Å precisely depicts the organization of a dimer of heterotrimers. Despite subtle surface remodeling and complete conservation of its active site with other homologues, MCR from the thermophile contains the most limited number of post-translational modifications reported so far, questioning their physiological relevance in other relatives. PubMed: 33919946DOI: 10.3390/microorganisms9040837 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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