ArticleThe Journal of biological chemistry2014
A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- Structural and mechanistic studies of the N-glycosylation machinery: from lipid-linked oligosaccharide biosynthesis to glycan transfer.Glycobiology · 2023Review
- The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon.Communications biology · 2021Article
- The Role of Substrate Mediated Allostery in the Catalytic Competency of the Bacterial Oligosaccharyltransferase PglB.Frontiers in molecular biosciences · 2021Article
- Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide.Scientific reports · 2018Article
- Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase.Nature communications · 2018Article
- Chemo-enzymatic synthesis of lipid-linked GlcNAc2Man5 oligosaccharides using recombinant Alg1, Alg2 and Alg11 proteins.Glycobiology · 2017Article
- Transmembrane motions of PglB induced by LLO are coupled with EL5 loop conformational changes necessary for OST activity.Glycobiology · 2017Article
- Characterization of the single-subunit oligosaccharyltransferase STT3A from Trypanosoma brucei using synthetic peptides and lipid-linked oligosaccharide analogs.Glycobiology · 2017Article
- Functional analysis of N-linking oligosaccharyl transferase enzymes encoded by deep-sea vent proteobacteria.Glycobiology · 2016Article
- Article
- Increased efficiency of Campylobacter jejuni N-oligosaccharyltransferase PglB by structure-guided engineering.Open biology · 2015Article
- Advances in understanding glycosyltransferases from a structural perspective.Current opinion in structural biology · 2014Review
- Substrate specificities and reaction kinetics of the yeast oligosaccharyltransferase isoforms.The Journal of biological chemistryArticle
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Asparagine-linked glycosylation is a post-translational protein modification that is conserved in all domains of life. The initial transfer of a lipid-linked oligosaccharide (LLO) onto acceptor asparagines is catalyzed by the integral membrane protein oligosaccharyltransferase (OST). The previously reported structure of a single-subunit OST enzyme, the Campylobacter lari protein PglB, revealed a partially disordered external loop (EL5), whose role in catalysis was unclear. We identified a new and functionally important sequence motif in EL5 containing a conserved tyrosine residue (Tyr293) whose aromatic side chain is essential for catalysis. A synthetic peptide containing the conserved motif can partially but specifically rescue in vitro activity of mutated PglB lacking Tyr293. Using site-directed disulfide cross-linking, we show that disengagement of the structurally ordered part of EL5 is an essential step of the glycosylation reaction, probably by allowing sequon binding or glyco-product release. Our findings define two distinct mechanistic roles of EL5 in OST-catalyzed glycosylation. These functions, exerted by the two halves of EL5, are independent, because the loop can be cleaved by specific proteolysis with only slight reduction in activity.
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