Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications
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<sub>430</sub>-cofactor as the catalyst. MCR astounds the scient...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-04-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/9/4/837 |
| _version_ | 1797537721156108288 |
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| author | Julia Maria Kurth Marie-Caroline Müller Cornelia Ulrike Welte Tristan Wagner |
| author_facet | Julia Maria Kurth Marie-Caroline Müller Cornelia Ulrike Welte Tristan Wagner |
| author_sort | Julia Maria Kurth |
| collection | DOAJ |
| description | 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<sub>430</sub>-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 <i>Methermicoccus shengliensis</i>. 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 <i>M. shengliensis</i> 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 <i>M. shengliensis</i> contains the most limited number of post-translational modifications reported so far, questioning their physiological relevance in other relatives. |
| first_indexed | 2024-03-10T12:19:27Z |
| format | Article |
| id | doaj.art-61ff87e6cb1842548689b4cab72ad736 |
| institution | Directory Open Access Journal |
| issn | 2076-2607 |
| language | English |
| last_indexed | 2024-03-10T12:19:27Z |
| publishDate | 2021-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Microorganisms |
| spelling | doaj.art-61ff87e6cb1842548689b4cab72ad7362023-11-21T15:35:19ZengMDPI AGMicroorganisms2076-26072021-04-019483710.3390/microorganisms9040837Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational ModificationsJulia Maria Kurth0Marie-Caroline Müller1Cornelia Ulrike Welte2Tristan Wagner3Department of Microbiology, Institute for Water and Wetland Research, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The NetherlandsMicrobial Metabolism Research Group, Max Planck Institute for Marine Microbiology, Celsiusstraße 1, 28359 Bremen, GermanyDepartment of Microbiology, Institute for Water and Wetland Research, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The NetherlandsMicrobial Metabolism Research Group, Max Planck Institute for Marine Microbiology, Celsiusstraße 1, 28359 Bremen, GermanyMethanogenic 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<sub>430</sub>-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 <i>Methermicoccus shengliensis</i>. 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 <i>M. shengliensis</i> 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 <i>M. shengliensis</i> contains the most limited number of post-translational modifications reported so far, questioning their physiological relevance in other relatives.https://www.mdpi.com/2076-2607/9/4/837methyl-coenzyme M reductasepost-translational modificationsmethoxydotrophic methanogenesisX-ray crystallographyF<sub>430</sub>-cofactorthermophilic archaeon |
| spellingShingle | Julia Maria Kurth Marie-Caroline Müller Cornelia Ulrike Welte Tristan Wagner Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications Microorganisms methyl-coenzyme M reductase post-translational modifications methoxydotrophic methanogenesis X-ray crystallography F<sub>430</sub>-cofactor thermophilic archaeon |
| title | Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications |
| title_full | Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications |
| title_fullStr | Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications |
| title_full_unstemmed | Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications |
| title_short | Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications |
| title_sort | structural insights into the methane generating enzyme from a methoxydotrophic methanogen reveal a restrained gallery of post translational modifications |
| topic | methyl-coenzyme M reductase post-translational modifications methoxydotrophic methanogenesis X-ray crystallography F<sub>430</sub>-cofactor thermophilic archaeon |
| url | https://www.mdpi.com/2076-2607/9/4/837 |
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