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TitleFunctional analysis of Ost3p and Ost6p containing yeast oligosaccharyltransferases.
Journal, issue, pagesGlycobiology, Vol. 31, Issue 12, Page 1604-1615, Year 2021
Publish dateDec 30, 2021
PubMed AbstractThe oligosaccharyltransferase (OST) is the central enzyme in the N-glycosylation pathway. It transfers a defined oligosaccharide from a lipid-linker onto the asparagine side chain of proteins. The ...The oligosaccharyltransferase (OST) is the central enzyme in the N-glycosylation pathway. It transfers a defined oligosaccharide from a lipid-linker onto the asparagine side chain of proteins. The yeast OST consists of eight subunits and exists in two catalytically distinct isoforms that differ in one subunit, Ost3p or Ost6p. The cryo-electron microscopy structure of the Ost6p containing complex was found to be highly similar to the Ost3p containing OST. OST enzymes with altered Ost3p/Ost6p subunits were generated and functionally analyzed. The three C-terminal transmembrane helices were responsible for the higher turnover-rate of the Ost3p vs. the Ost6p containing enzyme in vitro and the more severe hypoglycosylation in Ost3p lacking strains in vivo. Glycosylation of specific OST target sites required the N-terminal thioredoxin domain of Ost3p or Ost6p. This Ost3p/Ost6p dependence was glycosylation site but not protein specific. We concluded that the Ost3p/Ost6p subunits modulate the catalytic activity of OST and provide additional specificity for OST substrate recognition.
External linksGlycobiology / PubMed:34974622
MethodsEM (single particle)
Resolution3.46 Å
Structure data

12808

7oci

EMDB-12808, PDB-7oci:
Cryo-EM structure of yeast Ost6p containing oligosaccharyltransferase complex
Method: EM (single particle) / Resolution: 3.46 Å

Chemicals

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-AJP:
Digitonin / detergent*YM

ChemComp-MG:
Unknown entry

ChemComp-V8K:
Dolichylphosphate

Source
  • saccharomyces cerevisiae s288c (yeast)
KeywordsMEMBRANE PROTEIN / N-glycosylation / Yeast / Complex / Endoplasmic reticulum

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