7OCI
Cryo-EM structure of yeast Ost6p containing oligosaccharyltransferase complex
Summary for 7OCI
| Entry DOI | 10.2210/pdb7oci/pdb |
| EMDB information | 12808 |
| Descriptor | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 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, ... (16 entities in total) |
| Functional Keywords | n-glycosylation, yeast, complex, endoplasmic reticulum, membrane protein |
| Biological source | Saccharomyces cerevisiae S288C More |
| Total number of polymer chains | 9 |
| Total formula weight | 295172.02 |
| Authors | Wild, R.,Neuhaus, J.D.,Eyring, J.,Irobalieva, R.N.,Kowal, J.,Lin, C.W.,Locher, K.P.,Aebi, M. (deposition date: 2021-04-27, release date: 2022-02-16) |
| Primary citation | Neuhaus, J.D.,Wild, R.,Eyring, J.,Irobalieva, R.N.,Kowal, J.,Lin, C.W.,Locher, K.P.,Aebi, M. Functional analysis of Ost3p and Ost6p containing yeast oligosaccharyltransferases. Glycobiology, 31:1604-1615, 2021 Cited by PubMed Abstract: 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. PubMed: 34974622DOI: 10.1093/glycob/cwab084 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.46 Å) |
Structure validation
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