2LGZ
Solution structure of STT3P
Summary for 2LGZ
| Entry DOI | 10.2210/pdb2lgz/pdb |
| NMR Information | BMRB: 16701 |
| Descriptor | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 (1 entity in total) |
| Functional Keywords | catalytic domain, oligosaccharyl transferase, membrane protein, transferase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Membrane; Multi-pass membrane protein: P39007 |
| Total number of polymer chains | 1 |
| Total formula weight | 31412.99 |
| Authors | Huang, C.,Bhaskaran, R.,Mohanty, S. (deposition date: 2011-08-03, release date: 2012-08-01, Last modification date: 2024-05-15) |
| Primary citation | Huang, C.,Bhaskaran, R.,Mohanty, S. Eukaryotic N-Glycosylation Occurs via the Membrane-anchored C-terminal Domain of the Stt3p Subunit of Oligosaccharyltransferase. J.Biol.Chem., 287:32450-32458, 2012 Cited by PubMed Abstract: N-glycosylation is an essential and highly conserved protein modification. In eukaryotes, it is catalyzed by a multisubunit membrane-associated enzyme, oligosaccharyltransferase (OT). We report the high resolution structure of the C-terminal domain of eukaryotic Stt3p. Unlike its soluble β-sheet-rich prokaryotic counterparts, our model reveals that the C-terminal domain of yeast Stt3p is highly helical and has an overall oblate spheroid-shaped structure containing a membrane-embedded region. Anchoring of this protein segment to the endoplasmic reticulum membrane is likely to bring the membrane-embedded donor substrate closer, thus facilitating glycosylation efficiency. Structural comparison of the region near the WWDYG signature motif revealed that the acceptor substrate-binding site of yeast OT strikingly resembles its prokaryotic counterparts, suggesting a conserved mechanism of N-glycosylation from prokaryotes to eukaryotes. Furthermore, comparison of the NMR and cryo-EM structures of yeast OT revealed that the molecular architecture of this acceptor substrate-recognizing domain has interesting spatial specificity for interactions with other essential OT subunits. PubMed: 22865878DOI: 10.1074/jbc.M112.342253 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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