The crystal structure of an oligosaccharyltransferase in complex with a sugar donor and an acceptor peptide provides insight into the mechanism of protein glycosylation and reveals how lipid-linked oligosaccharides are positioned in the enzyme active site.
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The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon
Communications Biology Open Access 05 August 2021
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References
Napiórkowska, M. et al. Nat. Struct. Mol. Biol. 24, 1100–1106 (2017).
Gerber, S. et al. J. Biol. Chem. 288, 8849–8861 (2013).
Lizak, C. et al. Nat. Commun. 4, 2627 (2013).
Liu, F. et al. J. Am. Chem. Soc. 136, 566–569 (2014).
Lizak, C., Gerber, S., Numao, S., Aebi, M. & Locher, K.P. Nature 474, 350–355 (2011).
Matsumoto, S. et al. Proc. Natl. Acad. Sci. USA 110, 17868–17873 (2013).
Igura, M. et al. EMBO J. 27, 234–243 (2008).
Jaffee, M.B. & Imperiali, B. Biochemistry 50, 7557–7567 (2011).
Kelleher, D.J., Karaoglu, D., Mandon, E.C. & Gilmore, R. Mol. Cell 12, 101–111 (2003).
Karaoglu, D., Kelleher, D.J. & Gilmore, R. Biochemistry 40, 12193–12206 (2001).
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Shrimal, S., Cherepanova, N. & Gilmore, R. One flexible loop in OST lassos both substrates. Nat Struct Mol Biol 24, 1009–1010 (2017). https://doi.org/10.1038/nsmb.3508
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DOI: https://doi.org/10.1038/nsmb.3508