期刊
SCIENCE
卷 360, 期 6385, 页码 215-218出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar7899
关键词
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资金
- German Research Council [SFB646, GRK1721]
- NIH [GM35678]
- Center for Integrated Protein Science Munich (CiPS-M)
- European Research Council (Advanced Grant CRYOTRANSLATION)
- European Research Council under the European Union's Horizon Programme [ERC Consolidator Grant] [724425]
- Deutsche Forschungsgemeinschaft [FO 716/4-1]
- Boehringer Ingelheim Fonds
- European Research Council (ERC) [724425] Funding Source: European Research Council (ERC)
Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum by complex formation of a ribosome, the Sec61 protein-conducting channel, and oligosaccharyltransferase (OST). Here we used different cryo-electron microscopy approaches to determine structures of native and solubilized ribosome-Sec61-OST complexes. A molecular model for the catalytic OST subunit STT3A (staurosporine and temperature sensitive 3A) revealed how it is integrated into the OST and how STT3-paralog specificity for translocon-associated OST is achieved. The OST subunit DC2 was placed at the interface between Sec61 and STT3A, where it acts as a versatile module for recruitment of STT3A-containing OST to the ribosome-Sec61 complex. This detailed structural view on the molecular architecture of the cotranslational machinery for N-glycosylation provides the basis for a mechanistic understanding of glycoprotein biogenesis at the endoplasmic reticulum.
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