{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["McDowell MA"],"funding":["Deutsche Forschungsgemeinschaft (German Research Foundation)","Wellcome Trust"],"pagination":["11134"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12705809"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Protein O-mannosyltransferases (PMTs) are conserved endoplasmic reticulum membrane-embedded enzymes responsible for the transfer of mannose from dolichol phosphate-mannose (Dol-P-Man) to serine/threonine-rich protein substrates or unfolded proteins. PMTs from three subfamilies form obligate dimers with different substrate specificities and require the concerted action of their transmembrane domains (TMDs) and a luminal MIR domain for catalysis. Here, we present structures, native mass spectrometry, and structure-based mutagenesis of the fungal Pmt4 homodimer. The core fold of the TMDs and MIR domain is conserved with the Pmt1-Pmt2 heterodimer, indicating a shared catalytic mechanism. Distinct from Pmt4, the MIR domain interacts in cis with the TMDs of the same subunit and has a β-hairpin i"],"journal":["Nature communications"],"pubmed_title":["Structural characterisation of the fungal Pmt4 homodimer."],"pmcid":["PMC12705809"],"funding_grant_id":["221795/Z/20/Z","Leibniz Programme (SI 586/6-1), FOR2509 (SI 586/8-2)"],"pubmed_authors":["Bausewein D","Hackmann Y","Brenske D","Strahl S","Bilsing FL","McDowell MA","Fiorentino F","Wu D","Robinson CV","Mortensen S","Chiapparino A","Metschies A","Wild K","Sinning I"],"additional_accession":[]},"is_claimable":false,"name":"Structural characterisation of the fungal Pmt4 homodimer.","description":"Protein O-mannosyltransferases (PMTs) are conserved endoplasmic reticulum membrane-embedded enzymes responsible for the transfer of mannose from dolichol phosphate-mannose (Dol-P-Man) to serine/threonine-rich protein substrates or unfolded proteins. PMTs from three subfamilies form obligate dimers with different substrate specificities and require the concerted action of their transmembrane domains (TMDs) and a luminal MIR domain for catalysis. Here, we present structures, native mass spectrometry, and structure-based mutagenesis of the fungal Pmt4 homodimer. The core fold of the TMDs and MIR domain is conserved with the Pmt1-Pmt2 heterodimer, indicating a shared catalytic mechanism. Distinct from Pmt4, the MIR domain interacts in cis with the TMDs of the same subunit and has a β-hairpin i","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-07-15T06:39:06.26Z","creation":"2026-07-02T03:08:56.257Z"},"accession":"S-EPMC12705809","cross_references":{"pubmed":["41392315"],"doi":["10.1038/s41467-025-67412-1"]}}