Journal
GLYCOBIOLOGY
Volume 29, Issue 4, Pages 288-297Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwy093
Keywords
cotranslational glycosylation; lipid-linked oligosaccharide; N-glycosylation; oligosaccharyltransferase; OST structure
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Funding
- National Institute of General Medical Sciences of the National Institutes of Health [GM43768]
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Asparagine-linked (N-linked) glycosylation is one of the most common protein modification reactions in eukaryotic cells, occurring upon the majority of proteins that enter the secretory pathway. X-ray crystal structures of the single subunit OSTs from eubacterial and archaebacterial organisms revealed the location of donor and acceptor substrate binding sites and provided the basis for a catalytic mechanism. Cryoelectron microscopy structures of the octameric yeast OST provided substantial insight into the organization and assembly of the multisubunit oligosaccharyltransferases. Furthermore, the cryoelectron microscopy structure of a complex consisting of a mammalian OST complex, the protein translocation channel and a translating ribosome revealed new insight into the mechanism of cotranslational glycosylation.
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