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. Author manuscript; available in PMC: 2021 May 2.
Published in final edited form as: Nat Microbiol. 2020 Nov 2;6(1):19–26. doi: 10.1038/s41564-020-00798-4

Extended Data Fig. 7. β-barrels form a tight tether between the OM and PG.

Extended Data Fig. 7

Structural model of BbpA (red) in the C. burnetii OM. Structures of the cell envelope are colored as follows: inner leaflet of OM (grey), lipid A of LPS (orange), core oligosaccharides (yellow), glycan chains of PG (blue) peptide stems of PG (green). A similar model was generated for BbpB. b. Molecular dynamics simulation of C. burnetti OM-PG protein-tethered models. The distance in angstroms between the phosphorus atoms of the inner leaflet of the OM and PG layers was measured for three runs for BbpA, ala-BbpA, BbpB, LimB, and Lpp from E. coli. The solid lines are running averages. Distances measured in angstroms for run 1, run 2, and run 3 are shown.