ArticleScientific reports2016
MtrA of the sodium ion pumping methyltransferase binds cobalamin in a unique mode.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
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- Asgard archaea modulate potential methanogenesis substrates in wetland soil.Nature communications · 2024Article
- Structural and mechanistic basis of the central energy-converting methyltransferase complex of methanogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Understanding the sources, function, and irreplaceable role of cobamides in organohalide-respiring bacteria.Frontiers in microbiology · 2024Review
- Culexarchaeia, a novel archaeal class of anaerobic generalists inhabiting geothermal environments.ISME communications · 2022Article
- Archaeal Connectase is a specific and efficient protein ligase related to proteasome β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Methanogenesis involves direct hydride transfer from HNature reviews. Chemistry · 2020Review
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the three domains of life, vitamin B12 (cobalamin) is primarily used in methyltransferase and isomerase reactions. The methyltransferase complex MtrA-H of methanogenic archaea has a key function in energy conservation by catalysing the methyl transfer from methyl-tetrahydromethanopterin to coenzyme M and its coupling with sodium-ion translocation. The cobalamin-binding subunit MtrA is not homologous to any known B12-binding proteins and is proposed as the motor of the sodium-ion pump. Here, we present crystal structures of the soluble domain of the membrane-associated MtrA from Methanocaldococcus jannaschii and the cytoplasmic MtrA homologue/cobalamin complex from Methanothermus fervidus. The MtrA fold corresponds to the Rossmann-type α/β fold, which is also found in many cobalamin-containing proteins. Surprisingly, the cobalamin-binding site of MtrA differed greatly from all the other cobalamin-binding sites. Nevertheless, the hydrogen-bond linkage at the lower axial-ligand site of cobalt was equivalently constructed to that found in other methyltransferases and mutases. A distinct polypeptide segment fixed through the hydrogen-bond linkage in the relaxed Co(III) state might be involved in propagating the energy released upon corrinoid demethylation to the sodium-translocation site by a conformational change.
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