8AGC
Structure of yeast oligosaccharylransferase complex with lipid-linked oligosaccharide and non-acceptor peptide bound
Summary for 8AGC
| Entry DOI | 10.2210/pdb8agc/pdb |
| EMDB information | 15420 |
| Descriptor | Dolichyl-diphosphooligosaccharide--protein glycotransferase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (18 entities in total) |
| Functional Keywords | n-glycosylation ost complex, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 9 |
| Total formula weight | 297648.38 |
| Authors | Ramirez, A.S.,de Capitani, M.,Pesciullesi, G.,Kowal, J.,Bloch, J.S.,Irobalieva, R.N.,Aebi, M.,Reymond, J.L.,Locher, K.P. (deposition date: 2022-07-19, release date: 2022-12-07, Last modification date: 2023-10-18) |
| Primary citation | Ramirez, A.S.,de Capitani, M.,Pesciullesi, G.,Kowal, J.,Bloch, J.S.,Irobalieva, R.N.,Reymond, J.L.,Aebi, M.,Locher, K.P. Molecular basis for glycan recognition and reaction priming of eukaryotic oligosaccharyltransferase. Nat Commun, 13:7296-7296, 2022 Cited by PubMed Abstract: 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. PubMed: 36435935DOI: 10.1038/s41467-022-35067-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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