Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum
Copyright policy )Structural basis for coupling protein transport and N-glycosylation at the mammalian endoplasmic reticulum
A close-up view of oligosaccharyltransferase Many secretory and membrane proteins are modified through the attachment of sugar chains by N-glycosylation. Such modification is required for correct protein folding, targeting, and functionality. In mammalian cells, N-glycosylation is catalyzed by the oligosaccharyltransferase (OST) complex via its STT3 subunit. OST forms a complex with the ribosome and the Sec61 protein translocation channel. Braunger et al. combined cryo–electron microscopy approaches to visualize mammalian ribosome-Sec61-OST complexes in order to build an initial molecular model for mammalian OST. Science , this issue p. 215
- Ludwig-Maximilians-Universität München Germany
- Utrecht University Netherlands
- Max Planck Society Germany
- University of Massachusetts Medical School United States
- Max Planck Institute of Biochemistry Germany
Models, Molecular, Glycosylation, Protein Conformation, Research Support, Non-U.S. Gov't, Cryoelectron Microscopy, Molecular, Extramural, Membrane Proteins, Research Support, Endoplasmic Reticulum, N.I.H., Protein Transport, HEK293 Cells, Research Support, N.I.H., Extramural, Hexosyltransferases, Models, Taverne, Humans, Non-U.S. Gov't, Ribosomes, SEC Translocation Channels
Models, Molecular, Glycosylation, Protein Conformation, Research Support, Non-U.S. Gov't, Cryoelectron Microscopy, Molecular, Extramural, Membrane Proteins, Research Support, Endoplasmic Reticulum, N.I.H., Protein Transport, HEK293 Cells, Research Support, N.I.H., Extramural, Hexosyltransferases, Models, Taverne, Humans, Non-U.S. Gov't, Ribosomes, SEC Translocation Channels
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