PuSH - Publication Server of Helmholtz Zentrum München: Structure of the <em>Methanosarcina mazei</em> Mtr complex bound to the oxygen-stress responsive small protein MtrI.

Navigation

Home

Deutsch

Research

Advanced Search

Browse by ...

... Journal

... Publication Type

... Research Data

... Publication Year

Publication overview

Support & Contact

Contact persons

Help

Data protection

Reif-Trauttmansdorff, T.* ; Herdering, E.* ; Bohn, S. ; Pascoa, T.* ; Kahnt, J.* ; Zimmer, E.* ; Kumar, A.* ; Schmitz, R.A.* ; Schuller, J.M.*

Structure of the Methanosarcina mazei Mtr complex bound to the oxygen-stress responsive small protein MtrI.

Nat. Commun. 17:133 (2026)

Publ. Version/Full Text

Research data

DOI

PMC

	Open Access Gold

Abstract
Metrics
Extra information

Methanogenic archaea emit ~1 Gt of methane annually, impacting global carbon cycling and climate. Central to their energy metabolism is a membrane-bound, sodium-translocating methyltransferase complex: the N⁵-tetrahydromethanopterin:CoM-S-methyltransferase (Mtr). It couples methyl transfer between two methanogen-specific cofactors with sodium ion transport across the membrane, forming the only energy-conserving step in hydrogenotrophic methanogenesis. Here, we present a 2.1 Å single-particle cryo-EM structure of the Mtr complex from Methanosarcina mazei. The structure reveals the organization of all catalytic subunits, embedded archaeal lipids and the sodium-binding site. Most strikingly, we discover MtrI, a previously unannotated small open-reading frame encoded protein ( < 100 aa) found within the order of Methanosarcinales that binds both the top of the sodium-channel and cytosolic domain of MtrA via its cobamide cofactor in response to oxygen exposure. This interaction likely prevents sodium leakage and stabilizes the complex under oxidative conditions, revealing an unexpected regulatory mechanism in methanogen energy conservation.

Altmetric

Additional Metrics?

[➜Log in]

Edit extra informations Login

Publication type Article: Journal article

Document type Scientific Article

Keywords Sodium-ion Translocation; Methyltransferase Complex; Na+; Genome; Identification; Water

ISSN (print) / ISBN 2041-1723

e-ISSN 2041-1723

Journal Nature Communications

Quellenangaben Volume: 17, Issue: 1, Article Number: 133

Publisher Nature Publishing Group

Publishing Place London

Reviewing status Peer reviewed

Institute(s) Cryo-EM facility (CEMP)

Grants EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020)
Deutsche Forschungsgemeinschaft (German Research Foundation)