3GA4
Crystal structure of Ost6L (photoreduced form)
Summary for 3GA4
| Entry DOI | 10.2210/pdb3ga4/pdb |
| Related | 3G7Y 3G9B |
| Descriptor | Dolichyl-diphosphooligosaccharide-protein glycosyltransferase subunit OST6, TETRAETHYLENE GLYCOL, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, active site loop, redox state, membrane, transferase, transmembrane |
| Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
| Cellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein (Probable): Q03723 |
| Total number of polymer chains | 1 |
| Total formula weight | 20785.27 |
| Authors | Stirnimann, C.U.,Grimshaw, J.P.A.,Schulz, B.L.,Brozzo, M.S.,Fritsch, F.,Glockshuber, R.,Capitani, G.,Gruetter, M.G.,Aebi, M. (deposition date: 2009-02-16, release date: 2009-06-16, Last modification date: 2024-04-03) |
| Primary citation | Schulz, B.L.,Stirnimann, C.U.,Grimshaw, J.P.,Brozzo, M.S.,Fritsch, F.,Mohorko, E.,Capitani, G.,Glockshuber, R.,Grutter, M.G.,Aebi, M. Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency. Proc.Natl.Acad.Sci.USA, 106:11061-11066, 2009 Cited by PubMed Abstract: Asparagine-linked glycosylation is a common posttranslational modification of diverse secretory and membrane proteins in eukaryotes, where it is catalyzed by the multiprotein complex oligosaccharyltransferase. The functions of the protein subunits of oligoasccharyltransferase, apart from the catalytic Stt3p, are ill defined. Here we describe functional and structural investigations of the Ost3/6p components of the yeast enzyme. Genetic, biochemical and structural analyses of the lumenal domain of Ost6p revealed oxidoreductase activity mediated by a thioredoxin-like fold with a distinctive active-site loop that changed conformation with redox state. We found that mutation of the active-site cysteine residues of Ost6p and its paralogue Ost3p affected the glycosylation efficiency of a subset of glycosylation sites. Our results show that eukaryotic oligosaccharyltransferase is a multifunctional enzyme that acts at the crossroads of protein modification and protein folding. PubMed: 19549845DOI: 10.1073/pnas.0812515106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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