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  Structural and mechanistic basis of the central energy-converting methyltransferase complex of methanogenesis

Aziz, I., Kayastha, K., Kaltwasser, S., Vonck, J., Welsch, S., Murphy, B. J., et al. (2024). 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, 121(14): e2315568121. doi:10.1073/pnas.2315568121.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-000F-1828-A Versions-Permalink: https://hdl.handle.net/21.11116/0000-000F-182C-6
Genre: Zeitschriftenartikel
Alternativer Titel : Proceedings of the National Academy of Sciences

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externe Referenz:
https://doi.org/10.1073/pnas.2315568121 (Verlagsversion)
Beschreibung:
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OA-Status:
Hybrid

Urheber

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 Urheber:
Aziz, Iram1, Autor
Kayastha, Kanwal1, Autor
Kaltwasser, Susann1, Autor
Vonck, Janet1, Autor
Welsch, Sonja1, Autor
Murphy, Bonnie J.1, Autor
Kahnt, Jörg2, Autor           
Wu, Di1, Autor
Wagner, Tristan1, Autor
Shima, Seigo3, Autor                 
Ermler, Ulrich1, Autor
Affiliations:
1external, ou_persistent22              
2Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266266              
3Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              

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Schlagwörter: -
 Zusammenfassung: Methanogenic archaea inhabiting anaerobic environments play a crucial role in the global biogeochemical material cycle. The most universal electrogenic reaction of their methane-producing energy metabolism is catalyzed by N????5-methyl-tetrahydromethanopterin: coenzyme M methyltransferase (MtrABCDEFGH), which couples the vectorial Na+ transport with a methyl transfer between the one-carbon carriers tetrahydromethanopterin and coenzyme M via a vitamin B12 derivative (cobamide) as prosthetic group. We present the 2.08 Å cryo-EM structure of Mtr(ABCDEFG)3 composed of the central Mtr(ABFG)3 stalk symmetrically flanked by three membrane-spanning MtrCDE globes. Tetraether glycolipids visible in the map fill gaps inside the multisubunit complex. Putative coenzyme M and Na+ were identified inside or in a side-pocket of a cytoplasmic cavity formed within MtrCDE. Its bottom marks the gate of the transmembrane pore occluded in the cryo-EM map. By integrating Alphafold2 information, functionally competent MtrA?MtrH and MtrA?MtrCDE subcomplexes could be modeled and thus the methyl-tetrahydromethanopterin demethylation and coenzyme M methylation half-reactions structurally described. Methyl-transfer-driven Na+ transport is proposed to be based on a strong and weak complex between MtrCDE and MtrA carrying vitamin B12, the latter being placed at the entrance of the cytoplasmic MtrCDE cavity. Hypothetically, strongly attached methyl-cob(III)amide (His-on) carrying MtrA induces an inward-facing conformation, Na+ flux into the membrane protein center and finally coenzyme M methylation while the generated loosely attached (or detached) MtrA carrying cob(I)amide (His-off) induces an outward-facing conformation and an extracellular Na+ outflux. Methyl-cob(III)amide (His-on) is regenerated in the distant active site of the methyl-tetrahydromethanopterin binding MtrH implicating a large-scale shuttling movement of the vitamin B12-carrying domain.

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Sprache(n): eng - English
 Datum: 2024-03-26
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: URI: https://doi.org/10.1073/pnas.2315568121
DOI: 10.1073/pnas.2315568121
 Art des Abschluß: -

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Projektinformation

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Projektname : -
Grant ID : -
Förderprogramm : -
Förderorganisation : Max Planck Society
Projektname : -
Grant ID : -
Förderprogramm : Georg Forster stipend to I.A.
Förderorganisation : Humboldt foundation

Quelle 1

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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : PNAS
  Andere : Proceedings of the National Academy of Sciences of the USA
  Kurztitel : Proc. Natl. Acad. Sci. U. S. A.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 121 (14) Artikelnummer: e2315568121 Start- / Endseite: - Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230