date: 2021-04-14T13:02:07Z
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pdf:docinfo:title: Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications
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Keywords: methyl-coenzyme M reductase; post-translational modifications; methoxydotrophic methanogenesis; X-ray crystallography; F430-cofactor; thermophilic archaeon
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subject: 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 F430-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 Methermicoccus shengliensis. 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 M. shengliensis 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-Ċ 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 M. shengliensis contains the most limited number of post-translational modifications reported so far, questioning their physiological relevance in other relatives.
dc:creator: Julia Maria Kurth, Marie-Caroline Müller, Cornelia Ulrike Welte and Tristan Wagner
dcterms:created: 2021-04-14T12:52:23Z
Last-Modified: 2021-04-14T13:02:07Z
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title: Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications
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pdf:docinfo:keywords: methyl-coenzyme M reductase; post-translational modifications; methoxydotrophic methanogenesis; X-ray crystallography; F430-cofactor; thermophilic archaeon
pdf:docinfo:modified: 2021-04-14T13:02:07Z
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dc:title: Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications
modified: 2021-04-14T13:02:07Z
cp:subject: 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 F430-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 Methermicoccus shengliensis. 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 M. shengliensis 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-Ċ 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 M. shengliensis contains the most limited number of post-translational modifications reported so far, questioning their physiological relevance in other relatives.
pdf:docinfo:subject: 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 F430-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 Methermicoccus shengliensis. 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 M. shengliensis 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-Ċ 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 M. shengliensis contains the most limited number of post-translational modifications reported so far, questioning their physiological relevance in other relatives.
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pdf:docinfo:creator: Julia Maria Kurth, Marie-Caroline Müller, Cornelia Ulrike Welte and Tristan Wagner
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creator: Julia Maria Kurth, Marie-Caroline Müller, Cornelia Ulrike Welte and Tristan Wagner
meta:author: Julia Maria Kurth, Marie-Caroline Müller, Cornelia Ulrike Welte and Tristan Wagner
dc:subject: methyl-coenzyme M reductase; post-translational modifications; methoxydotrophic methanogenesis; X-ray crystallography; F430-cofactor; thermophilic archaeon
meta:creation-date: 2021-04-14T12:52:23Z
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meta:keyword: methyl-coenzyme M reductase; post-translational modifications; methoxydotrophic methanogenesis; X-ray crystallography; F430-cofactor; thermophilic archaeon
Author: Julia Maria Kurth, Marie-Caroline Müller, Cornelia Ulrike Welte and Tristan Wagner
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