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DTSTART:20190331T030000
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DTSTART:20181028T020000
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BEGIN:VEVENT
DTSTAMP:20260403T220446Z
UID:5c2646e92bcc7898237610@ist.ac.at
DTSTART:20190121T100000
DTEND:20190121T110000
DESCRIPTION:Speaker: Rebekka Wild\nhosted by Eva Benkova\nAbstract: The cen
 tral enzyme in the N-glycosylation pathway is the oligosaccharyltransferas
 e (OST)\, which catalyzes the transfer of a lipid-linked oligosaccharide o
 nto peptide substrates. We determined the structure of the yeast octa-subu
 nit OST complex to uncover the function of the different subunits\, their 
 structures and their assembly into the complex (Wild\, Kowal\, Eyring et a
 l.\, Science\, 2018). Our single-particle cryo-EM structure at 3.3 resolut
 ion reveals that the STT3 subunit harbors the catalytic center\, which fac
 es away from the other subunits\, thereby allowing unhindered access to th
 e lipid-linked oligosaccharide and peptide substrates. The non-catalytic s
 ubunits form a rigid scaffold providing additional binding surfaces for su
 bstrate recognition and for potential protein interaction partners. Of not
 e\, our high-resolution OST structure fits well into a previously publishe
 d cryo-electron tomography map of the mammalian OST-translocon-ribosome co
 mplex. The docking analyses reveal an orientation of the OST complex with 
 its catalytic site facing the translocon. This architecture allows OST to 
 efficiently glycosylate native peptide chains entering the ER through the 
 translocon.
LOCATION:Mondi Seminar Room 2\, Central Building\, ISTA
ORGANIZER:tguggenb@ist.ac.at
SUMMARY:Rebekka Wild: Insights into N-linked protein glycosylation from cry
 o-EM studies on the yeast oligosaccharyltransferase complex
URL:https://talks-calendar.ista.ac.at/events/1716
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