{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Reif-Trauttmansdorff T"],"funding":["Deutsche Forschungsgemeinschaft","Deutsche Forschungsgemeinschaft (German Research Foundation)","EC | Horizon 2020 Framework Programme","EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020)"],"pagination":["133"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12774963"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(1)"],"pubmed_abstract":["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 "],"journal":["Nature communications"],"pubmed_title":["Structure of the Methanosarcina mazei Mtr complex bound to the oxygen-stress responsive small protein MtrI."],"pmcid":["PMC12774963"],"funding_grant_id":["RTG 2937","SCHU 3364/1-1","101075992"],"pubmed_authors":["Kahnt J","Zimmer E","Herdering E","Pascoa T","Reif-Trauttmansdorff T","Bohn S","Schmitz RA","Schuller JM","Kumar A"],"additional_accession":[]},"is_claimable":false,"name":"Structure of the Methanosarcina mazei Mtr complex bound to the oxygen-stress responsive small protein MtrI.","description":"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 ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-07-15T13:28:43.162Z","creation":"2026-07-05T03:08:35.748Z"},"accession":"S-EPMC12774963","cross_references":{"pubmed":["41436738"],"doi":["10.1038/s41467-025-67705-5"]}}