Journal
BIOPHYSICAL JOURNAL
Volume 107, Issue 8, Pages 1885-1895Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2014.09.007
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Funding
- NSF [MCB-1157677, ABI-1145987, DBI-1145652]
- HFSP [RGP0064/2011]
- XSEDE [MCB070009]
- K-INBRE [NIH P20 GM103418]
- KU undergraduate research award
- NIH [GM070855, GM072558]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1157677] Funding Source: National Science Foundation
- Div Of Biological Infrastructure
- Direct For Biological Sciences [1145652, 1145987] Funding Source: National Science Foundation
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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 (Glc(3)-Man(9)-GIcNAc(2)-PP-Dolichol) and bacterial (Glc(1)-GaINAc5-Bac(1)-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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