ArticleBiophysical journal2014
Lipid-linked oligosaccharides in membranes sample conformations that facilitate binding to oligosaccharyltransferase.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
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- The cryo-EM structure of the bd oxidase from M. tuberculosis reveals a unique structural framework and enables rational drug design to combat TB.Nature communications · 2021Article
- Review
- Enzymatic trans-bilayer lipid transport: Mechanisms, efficiencies, slippage, and membrane curvature.Biochimica et biophysica acta. Biomembranes · 2021Review
- Nonenzymatic synthesis of anomerically pure, mannosyl-based molecular probes for scramblase identification studies.Beilstein journal of organic chemistry · 2020Article
- Investigation of the conserved reentrant membrane helix in the monotopic phosphoglycosyl transferase superfamily supports key molecular interactions with polyprenol phosphate substrates.Archives of biochemistry and biophysics · 2019Article
- Inward-facing conformation of a multidrug resistance MATE family transporter.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Probing key elements of teixobactin-lipid II interactions in membranes.Chemical science · 2018Article
- Article
- Transmembrane motions of PglB induced by LLO are coupled with EL5 loop conformational changes necessary for OST activity.Glycobiology · 2017Article
- Probing Polytopic Membrane Protein-Substrate Interactions by Luminescence Resonance Energy Transfer.Journal of the American Chemical Society · 2016Article
- Structural biology: Lipid gymnastics.Nature · 2015Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Lipid-linked oligosaccharides (LLOs) are the substrates of oligosaccharyltransferase (OST), the enzyme that catalyzes the en bloc transfer of the oligosaccharide onto the acceptor asparagine of nascent proteins during the process of N-glycosylation. To explore LLOs' preferred location, orientation, structure, and dynamics in membrane bilayers of three different lipid types (dilauroylphosphatidylcholine, dimyristoylphosphatidylcholine, and dioleoylphosphatidylcholine), we have modeled and simulated both eukaryotic (Glc3-Man9-GlcNAc2-PP-Dolichol) and bacterial (Glc1-GalNAc5-Bac1-PP-Undecaprenol) LLOs, which are composed of an isoprenoid moiety and an oligosaccharide, linked by pyrophosphate. The simulations show no strong impact of different bilayer hydrophobic thicknesses on the overall orientation, structure, and dynamics of the isoprenoid moiety and the oligosaccharide. The pyrophosphate group stays in the bilayer head group region. The isoprenoid moiety shows high flexibility inside the bilayer hydrophobic core, suggesting its potential role as a tentacle to search for OST. The oligosaccharide conformation and dynamics are similar to those in solution, but there are preferred interactions between the oligosaccharide and the bilayer interface, which leads to LLO sugar orientations parallel to the bilayer surface. Molecular docking of the bacterial LLO to a bacterial OST suggests that such orientations can enhance binding of LLOs to OST.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.