Schwarz, F. & Aebi, M. Mechanisms and principles of N-linked protein glycosylation. Curr. Opin. Struct. Biol. 21, 576–582 (2011).
Nothaft, H. & Szymanski, C.M. Protein glycosylation in bacteria: sweeter than ever. Nat. Rev. Microbiol. 8, 765–778 (2010).
Calo, D., Kaminski, L. & Eichler, J. Protein glycosylation in Archaea: sweet and extreme. Glycobiology 20, 1065–1076 (2010).
Szymanski, C.M., Yao, R., Ewing, C.P., Trust, T.J. & Guerry, P. Evidence for a system of general protein glycosylation in Campylobacter jejuni. Mol. Microbiol. 32, 1022–1030 (1999).
Helenius, A. & Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73, 1019–1049 (2004).
Kornfeld, R. & Kornfeld, S. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631–664 (1985).
Cherepanova, N., Shrimal, S. & Gilmore, R. N-linked glycosylation and homeostasis of the endoplasmic reticulum. Curr. Opin. Cell Biol. 41, 57–65 (2016).
Nothaft, H. & Szymanski, C.M. Bacterial protein N-glycosylation: new perspectives and applications. J. Biol. Chem. 288, 6912–6920 (2013).
Valguarnera, E., Kinsella, R.L. & Feldman, M.F. Sugar and spice make bacteria not nice: protein glycosylation and its influence in pathogenesis. J. Mol. Biol. 428, 3206–3220 (2016).
Wacker, M. et al. Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems. Proc. Natl. Acad. Sci. USA 103, 7088–7093 (2006).
Marshall, R.D. Glycoproteins. Annu. Rev. Biochem. 41, 673–702 (1972).
Lairson, L.L., Henrissat, B., Davies, G.J. & Withers, S.G. Glycosyltransferases: structures, functions, and mechanisms. Annu. Rev. Biochem. 77, 521–555 (2008).
Liu, J. & Mushegian, A. Three monophyletic superfamilies account for the majority of the known glycosyltransferases. Protein Sci. 12, 1418–1431 (2003).
Kelleher, D.J. & Gilmore, R. An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology 16, 47R–62R (2006).
Yan, Q. & Lennarz, W.J. Studies on the function of oligosaccharyl transferase subunits: a glycosylatable photoprobe binds to the luminal domain of Ost1p. Proc. Natl. Acad. Sci. USA 99, 15994–15999 (2002).
Nasab, F.P., Schulz, B.L., Gamarro, F., Parodi, A.J. & Aebi, M. All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae. Mol. Biol. Cell 19, 3758–3768 (2008).
Lizak, C., Gerber, S., Numao, S., Aebi, M. & Locher, K.P. X-ray structure of a bacterial oligosaccharyltransferase. Nature 474, 350–355 (2011).
Matsumoto, S. et al. Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. Proc. Natl. Acad. Sci. USA 110, 17868–17873 (2013).
Matsumoto, S., Taguchi, Y., Shimada, A., Igura, M. & Kohda, D. Tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex. Biochemistry 56, 602–611 (2017).
Gerber, S. et al. Mechanism of bacterial oligosaccharyltransferase: in vitro quantification of sequon binding and catalysis. J. Biol. Chem. 288, 8849–8861 (2013).
Lizak, C. et al. Unexpected reactivity and mechanism of carboxamide activation in bacterial N-linked protein glycosylation. Nat. Commun. 4, 2627 (2013).
Bause, E., Breuer, W. & Peters, S. Investigation of the active site of oligosaccharyltransferase from pig liver using synthetic tripeptides as tools. Biochem. J. 312, 979–985 (1995).
Imperiali, B., Shannon, K.L. & Rickert, K.W. Role of peptide conformation in asparagine-linked glycosylation. J. Am. Chem. Soc. 114, 7942–7944 (1992).
Imperiali, B. & Tai, V.W. in Carbohydrate-Based Drug Discovery (ed. C.-H. Wong) 281–303 (Wiley-VCH, 2003).
Liu, F. et al. Rationally designed short polyisoprenol-linked PglB substrates for engineered polypeptide and protein N-glycosylation. J. Am. Chem. Soc. 136, 566–569 (2014).
Musumeci, M.A. et al. In vitro activity of Neisseria meningitidis PglL O-oligosaccharyltransferase with diverse synthetic lipid donors and a UDP-activated sugar. J. Biol. Chem. 288, 10578–10587 (2013).
Compain, P. & Martin, O.R. Carbohydrate mimetics-based glycosyltransferase inhibitors. Bioorg. Med. Chem. 9, 3077–3092 (2001).
Ramírez, A.S. et al. Characterization of the single-subunit oligosaccharyltransferase STT3A from Trypanosoma brucei using synthetic peptides and lipid-linked oligosaccharide analogs. Glycobiology 27, 525–535 (2017).
Hajduch, J. et al. A convenient synthesis of the C-1-phosphonate analogue of UDP-GlcNAc and its evaluation as an inhibitor of O-linked GlcNAc transferase (OGT). Carbohydr. Res. 343, 189–195 (2008).
Knapp, S. & Myers, D.S. α-GlcNAc thioconjugates. J. Org. Chem. 66, 3636–3638 (2001).
Knapp, S. & Ajayi, K. The anomeric Pudovik rearrangement. Tetrahedr. Lett. 48, 1945–1949 (2007).
Knapp, S., Gonzalez, S., Myers, D.S., Eckman, L.L. & Bewley, C.A. Shortcut to mycothiol analogues. Org. Lett. 4, 4337–4339 (2002).
Engel, R. Phosphonates as analogues of natural phosphates. Chem. Rev. 77, 349–367 (1977).
Jaffee, M.B. & Imperiali, B. Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases. Biochemistry 50, 7557–7567 (2011).
Ihssen, J. et al. Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB. BMC Biotechnol. 12, 67 (2012).
Lizak, C. et al. A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB. J. Biol. Chem. 289, 735–746 (2014).
Weerapana, E., Glover, K.J., Chen, M.M. & Imperiali, B. Investigating bacterial N-linked glycosylation: synthesis and glycosyl acceptor activity of the undecaprenyl pyrophosphate-linked bacillosamine. J. Am. Chem. Soc. 127, 13766–13767 (2005).
Glover, K.J., Weerapana, E. & Imperiali, B. In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proc. Natl. Acad. Sci. USA 102, 14255–14259 (2005).
Igura, M. et al. Structure-guided identification of a new catalytic motif of oligosaccharyltransferase. EMBO J. 27, 234–243 (2008).
Pedebos, C., Arantes, P.R., Giesel, G.M. & Verli, H. In silico investigation of the PglB active site reveals transient catalytic states and octahedral metal ion coordination. Glycobiology 25, 1183–1195 (2015).
Lee, S.H. & Im, W. Transmembrane motions of PglB induced by LLO are coupled with EL5 loop conformational changes necessary for OST activity. Glycobiology 27, 734–742 (2017).
Kabsch, W. Xds. Acta Crystallogr. D Biol. Crystallogr. 66, 125–132 (2010).
Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D. Biol. Crystallogr. 60, 2126–2132 (2004).
Adams, P.D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D. Biol. Crystallogr. 58, 1948–1954 (2002).
DeLano, W.L. The PyMOL Molecular Graphics System (DeLano Scientific, 2002).
Kowarik, M. et al. N-linked glycosylation of folded proteins by the bacterial oligosaccharyltransferase. Science 314, 1148–1150 (2006).
Perez, C. et al. Structure and mechanism of an active lipid-linked oligosaccharide flippase. Nature 524, 433–438 (2015).
