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

ABSTRACT: 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 multisubuni

SUBMITTER: Aziz I 

PROVIDER: S-EPMC10998594 | biostudies-literature | 2024 Apr

REPOSITORIES: biostudies-literature