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Eukaryotic N-Glycosylation Occurs via the Membrane-anchored C-terminal Domain of the Stt3p Subunit of Oligosaccharyltransferase


Metadata FieldValueLanguage
dc.creatorHuang, Chengdong
dc.creatorBhaskaran, Rajagopalan
dc.creatorMohanty, Smita
dc.date.accessioned2020-07-24T19:10:17Z
dc.date.available2020-07-24T19:10:17Z
dc.date.created2012
dc.identifier10.1074/jbc.M112.342253en_US
dc.identifier.urihttps://europepmc.org/articles/pmc3463301/bin/supp_m112.342253_jbc.m112.342253-1.pdfen_US
dc.identifier.urihttps://aurora.auburn.edu//handle/11200/49917
dc.identifier.urihttp://dx.doi.org/10.35099/aurora-5
dc.description.abstractN-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 -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.en_US
dc.formatPDFen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.relation.ispartofseries0021-9258en_US
dc.titleEukaryotic N-Glycosylation Occurs via the Membrane-anchored C-terminal Domain of the Stt3p Subunit of Oligosaccharyltransferaseen_US
dc.typeTexten_US
dc.type.genreJournal Article, Academic Journalen_US
dc.citation.volume287en_US
dc.citation.issue39en_US
dc.citation.spage32450en_US
dc.citation.epage32458en_US
dc.description.statusPublisheden_US
dc.description.peerreviewyesen_US

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