1. (CSDB ID: 48606) | ![]() |
a-D-Manp-(1-6)-+ | a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-2)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (Stt3p)/ | Show graphically |
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Saccharomyces cerevisiae ATCC 204508 / S288c
(Ancestor NCBI TaxID 4932,
species name lookup)
N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalysed by an eight-protein oligosaccharyltransferase (OST) complex that is embedded in the endoplasmic reticulum membrane. Our understanding of eukaryotic protein N-glycosylation has been limited owing to the lack of high-resolution structures. Here we report a 3.5 Å resolution cryo-electron microscopy structure of the Saccharomyces cerevisiae OST complex, revealing the structures of subunits Ost1-Ost5, Stt3, Wbp1 and Swp1. We found that seven phospholipids mediate many of the inter-subunit interactions, and an Stt3 N-glycan mediates interactions with Wbp1 and Swp1 in the lumen. Ost3 was found to mediate the OST-Sec61 translocon interface, funnelling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon. The structure provides insights into co-translational protein N-glycosylation, and may facilitate the development of small-molecule inhibitors that target this process.
structure, oligosaccharyltransferase, Saccharomyces cerevisiae, cryo-electron microscopy, N-glycosilation
Structure type: oligomer
2. (CSDB ID: 48607) | ![]() |
b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (Ost1p)/ | Show graphically |
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Saccharomyces cerevisiae ATCC 204508 / S288c
(Ancestor NCBI TaxID 4932,
species name lookup)
N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalysed by an eight-protein oligosaccharyltransferase (OST) complex that is embedded in the endoplasmic reticulum membrane. Our understanding of eukaryotic protein N-glycosylation has been limited owing to the lack of high-resolution structures. Here we report a 3.5 Å resolution cryo-electron microscopy structure of the Saccharomyces cerevisiae OST complex, revealing the structures of subunits Ost1-Ost5, Stt3, Wbp1 and Swp1. We found that seven phospholipids mediate many of the inter-subunit interactions, and an Stt3 N-glycan mediates interactions with Wbp1 and Swp1 in the lumen. Ost3 was found to mediate the OST-Sec61 translocon interface, funnelling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon. The structure provides insights into co-translational protein N-glycosylation, and may facilitate the development of small-molecule inhibitors that target this process.
structure, oligosaccharyltransferase, Saccharomyces cerevisiae, cryo-electron microscopy, N-glycosilation
Structure type: oligomer
3. (CSDB ID: 48608) | ![]() |
b-D-GlcpNAc-(1--/(->4) Asn-X-Ser/Thr (Wbp1p)/ | Show graphically |
Show legend Show as text |
Saccharomyces cerevisiae ATCC 204508 / S288c
(Ancestor NCBI TaxID 4932,
species name lookup)
N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalysed by an eight-protein oligosaccharyltransferase (OST) complex that is embedded in the endoplasmic reticulum membrane. Our understanding of eukaryotic protein N-glycosylation has been limited owing to the lack of high-resolution structures. Here we report a 3.5 Å resolution cryo-electron microscopy structure of the Saccharomyces cerevisiae OST complex, revealing the structures of subunits Ost1-Ost5, Stt3, Wbp1 and Swp1. We found that seven phospholipids mediate many of the inter-subunit interactions, and an Stt3 N-glycan mediates interactions with Wbp1 and Swp1 in the lumen. Ost3 was found to mediate the OST-Sec61 translocon interface, funnelling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon. The structure provides insights into co-translational protein N-glycosylation, and may facilitate the development of small-molecule inhibitors that target this process.
structure, oligosaccharyltransferase, Saccharomyces cerevisiae, cryo-electron microscopy, N-glycosilation
Structure type: monomerNew query | Export IDs | Home | Help |
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