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Structure paper

TitleMolecular basis for glycan recognition and reaction priming of eukaryotic oligosaccharyltransferase.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 7296, Year 2022
Publish dateNov 26, 2022
AuthorsAna S Ramírez / Mario de Capitani / Giorgio Pesciullesi / Julia Kowal / Joël S Bloch / Rossitza N Irobalieva / Jean-Louis Reymond / Markus Aebi / Kaspar P Locher /
PubMed AbstractOligosaccharyltransferase (OST) is the central enzyme of N-linked protein glycosylation. It catalyzes the transfer of a pre-assembled glycan, GlcNAcManGlc, from a dolichyl-pyrophosphate donor to ...Oligosaccharyltransferase (OST) is the central enzyme of N-linked protein glycosylation. It catalyzes the transfer of a pre-assembled glycan, GlcNAcManGlc, from a dolichyl-pyrophosphate donor to acceptor sites in secretory proteins in the lumen of the endoplasmic reticulum. Precise recognition of the fully assembled glycan by OST is essential for the subsequent quality control steps of glycoprotein biosynthesis. However, the molecular basis of the OST-donor glycan interaction is unknown. Here we present cryo-EM structures of S. cerevisiae OST in distinct functional states. Our findings reveal that the terminal glucoses (Glc) of a chemo-enzymatically generated donor glycan analog bind to a pocket formed by the non-catalytic subunits WBP1 and OST2. We further find that binding either donor or acceptor substrate leads to distinct primed states of OST, where subsequent binding of the other substrate triggers conformational changes required for catalysis. This alternate priming allows OST to efficiently process closely spaced N-glycosylation sites.
External linksNat Commun / PubMed:36435935 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.3 Å
Structure data

15419

8agb

EMDB-15419, PDB-8agb:
Structure of yeast oligosaccharylransferase complex with lipid-linked oligosaccharide bound
Method: EM (single particle) / Resolution: 3.0 Å

15420

8agc

EMDB-15420, PDB-8agc:
Structure of yeast oligosaccharylransferase complex with lipid-linked oligosaccharide and non-acceptor peptide bound
Method: EM (single particle) / Resolution: 3.1 Å

15421

8age

EMDB-15421, PDB-8age:
Structure of yeast oligosaccharylransferase complex with acceptor peptide bound
Method: EM (single particle) / Resolution: 2.8 Å

4161

6ezn

EMDB-4161, PDB-6ezn:
Cryo-EM structure of the yeast oligosaccharyltransferase (OST) complex
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-CPL:
1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM / Phosphatidylcholine

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM / Phosphatidylethanolamine

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-MN:
Unknown entry

ChemComp-ELU:
phosphono [(3~{R},6~{E},10~{E})-3,7,11,15-tetramethylhexadeca-6,10,14-trienyl] hydrogen phosphate

ChemComp-323:
2-[3,6-bis(dimethylamino)xanthen-9-yl]-5-methanoyl-benzoate

ChemComp-KZB:
(2~{S},3~{R},4~{R},5~{S},6~{S})-2-(hydroxymethyl)-6-[(1~{S},2~{R},3~{R},4~{R},5'~{S},6~{S},7~{R},8~{S},9~{R},12~{R},13~{R},15~{S},16~{S},18~{R})-5',7,9,13-tetramethyl-3,15-bis(oxidanyl)spiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icosane-6,2'-oxane]-16-yl]oxy-oxane-3,4,5-triol

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • Baker's yeast (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsMEMBRANE PROTEIN / OST complex / oligosaccharyltransferase / N-linked glycosylation / yeast / TRANSFERASE / N-glycosylation OST complex

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