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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. PNAS. doi:10.1073/pnas.2315568121.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-000F-6988-2 Versions-Permalink: https://hdl.handle.net/21.11116/0000-000F-6989-1
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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, Jörg1, Autor
Wu, Di1, Autor
Wagner, Tristan2, Autor           
Shima, Seigo1, Autor
Ermler, Ulrich1, Autor
Affiliations:
1external, ou_persistent22              
2Research Group Microbial Metabolism, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_3282402              

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 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 N5-methyl-tetrahydromethanopterin:
coenzyme M methyltransferase (MtrABCDEFGH), which couples the vectorial Na+
transport with a methyl transfer between the one-carbon carriers tetrahydromethano-
pterin 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 cen-
tral 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 cytoplas-
mic cavity formed within MtrCDE. Its bottom marks the gate of the transmembrane
pore occluded in the cryo-EM map. By integrating Alphafold2 information, function-
ally competent MtrA–MtrH and MtrA–MtrCDE subcomplexes could be modeled and
thus the methyl-tetrahydromethanopterin demethylation and coenzyme M methyla-
tion half-reactions structurally described. Methyl-transfer-driven Na+ transport is pro-
posed 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 car-
rying 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: Online veröffentlicht
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: DOI: 10.1073/pnas.2315568121
 Art des Abschluß: -

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Titel: PNAS
  Andere : Proceedings of the National Academy of Sciences of the United States of America
  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: - Artikelnummer: - Start- / Endseite: - Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230