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TitleStructural characterisation of the fungal Pmt4 homodimer.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 11134, Year 2025
Publish dateDec 14, 2025
AuthorsMelanie A McDowell / Klemens Wild / Francesco Fiorentino / Daniela Bausewein / Anke Metschies / Antonella Chiapparino / Yvonne Hackmann / Florestan L Bilsing / David Brenske / Sofia Mortensen / Di Wu / Carol V Robinson / Sabine Strahl / Irmgard Sinning /
PubMed AbstractProtein O-mannosyltransferases (PMTs) are conserved endoplasmic reticulum membrane-embedded enzymes responsible for the transfer of mannose from dolichol phosphate-mannose (Dol-P-Man) to ...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 insertion required for O-mannosylation of substrates. We further identify a cytosolic binding site for substrate Dol-P-Man within the Pmt4 TMDs, which is conserved amongst PMTs and important for in vivo activity. Thus, we provide a framework to understand the substrate specificity and regulation of the Pmt4 homodimer.
External linksNat Commun / PubMed:41392315 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.22 - 3.4 Å
Structure data

52631

9i5k

EMDB-52631, PDB-9i5k:
Structure of the Chaetomium thermophilum Pmt4 homodimer (C2 symmetry)
Method: EM (single particle) / Resolution: 3.2 Å

52632

9i5l

EMDB-52632, PDB-9i5l:
Structure of the Chaetomium thermophilum Pmt4 homodimer (C1 symmetry)
Method: EM (single particle) / Resolution: 3.4 Å

PDB-9fd0:
Structure of the Saccharomyces cerevisiae Pmt4-MIR domain with bound ligands
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-9fd1:
Structure of the Chaetomium thermophilum Pmt4-MIR domain with bound ligands
Method: X-RAY DIFFRACTION / Resolution: 1.22 Å

Chemicals

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ACT:
ACETATE ION

ChemComp-NA:
Unknown entry

PDB-1i0n:
1.3 A STRUCTURE OF THE A-DECAMER GCGTATACGC WITH A SINGLE 2'-O-METHYL-[TRI(OXYETHYL)] THYMINE IN PLACE OF T6, MEDIUM RB-SALT

PDB-1i0m:
1.05 A STRUCTURE OF THE A-DECAMER GCGTATACGC WITH A SINGLE 2'-O-FLUOROETHYL THYMINE IN PLACE OF T6, HIGH RB-SALT

Source
  • thermochaetoides thermophila (fungus)
  • saccharomyces cerevisiae (brewer's yeast)
  • chaetomium (fungus)
KeywordsPEPTIDE BINDING PROTEIN / Protein O-mannosylation / glycosylation / ER luminal domain / b-trefoil / ligand binding / processivity / thermostability / MEMBRANE PROTEIN / homodimer / ER / biogenesis

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