6FTI
Cryo-EM Structure of the Mammalian Oligosaccharyltransferase Bound to Sec61 and the Programmed 80S Ribosome
This is a non-PDB format compatible entry.
Summary for 6FTI
Entry DOI | 10.2210/pdb6fti/pdb |
EMDB information | 4306 4307 4308 4309 4310 4311 4312 4313 4314 4315 4316 4317 |
Descriptor | uL2, Ribosomal protein L11, eL13, ... (64 entities in total) |
Functional Keywords | protein translocon of the endoplasmic reticulum, protein transport |
Biological source | Oryctolagus cuniculus (Rabbit) More |
Total number of polymer chains | 60 |
Total formula weight | 2289695.84 |
Authors | Braunger, K.,Becker, T.,Beckmann, R. (deposition date: 2018-02-22, release date: 2018-03-21, Last modification date: 2020-07-29) |
Primary citation | Braunger, K.,Pfeffer, S.,Shrimal, S.,Gilmore, R.,Berninghausen, O.,Mandon, E.C.,Becker, T.,Forster, F.,Beckmann, R. Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum. Science, 360:215-219, 2018 Cited by PubMed Abstract: 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. PubMed: 29519914DOI: 10.1126/science.aar7899 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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