PDBe 6p2r

Electron Microscopy
3.2Å resolution

Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor

Released:
Primary publication:
Structure of the eukaryotic protein O-mannosyltransferase Pmt1-Pmt2 complex.
Nat. Struct. Mol. Biol. (2019)
PMID: 31285605
Related structures: EMD-20240

Function and Biology Details

Reaction catalysed:
Dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dolichyl-phosphate-mannose--protein mannosyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 817 amino acids
Theoretical weight: 92.77 KDa
Source organism: Saccharomyces cerevisiae W303
Expression system: Saccharomyces cerevisiae W303
UniProt:
  • Canonical: P33775 (Residues: 1-817; Coverage: 100%)
Gene names: D2390, PMT1, YDL095W
Sequence domains:
Dolichyl-phosphate-mannose--protein mannosyltransferase 2 Chain: B
Molecule details ›
Chain: B
Length: 759 amino acids
Theoretical weight: 86.96 KDa
Source organism: Saccharomyces cerevisiae W303
Expression system: Saccharomyces cerevisiae W303
UniProt:
  • Canonical: P31382 (Residues: 1-759; Coverage: 100%)
Gene names: FUN25, PMT2, YAL023C
Sequence domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.2Å
Relevant EMDB volumes: EMD-20240
Expression system: Saccharomyces cerevisiae W303