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. 2022 Feb 14;7(3):397–410. doi: 10.1038/s41564-022-01059-2

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© The Author(s) 2022, corrected publication 2022

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Fig. 3 — a, Side (left) and cutaway (right) views of ribbon diagrams showing the overall structure of the central part of the AlgoCIS baseplate. The colour code matches Fig. 1d, while the PAAR-like Alg10 is represented by the dashed triangle. The box indicates the position of trimeric plug protein Alg6, which is shown in d. b, Schematic and ribbon diagrams showing that Alg8 has three domains. The N and C termini are marked with red and green circles. c, Left: structural superpositions of Alg8 (red) and homologues (Afp8, blue; Pvc8, green) based on the gp27-like domain showing the different domain organization in the Alg8 protein compared with the homologues. Right: perpendicular view of the dashed box on the left. The black triangle indicates the symmetry axis. d, Top: shadowed surface and ribbon diagrams showing the plug (trimeric Alg6) localization inside the tube-exposed cavity of the central spike. The corresponding densities surround one Alg6 protein are coloured transparent blue. The positions of the flexible linker, N and C termini are labelled. Bottom: ribbon diagrams of perpendicular slices (positions 1 and 2 in the top panel), revealing that the hydrophobic core of the Alg6 trimer exposes charged residues on the outer surface. e, Negative-stain EM images of purified MACs from wild-type P. luteoviolacea and mutant ΔJF50_12690, showing aberrant MAC tail structures (highlighted by white arrowheads) in the strain with deleted Alg6 homologue (JF50_12690). This experiment was performed three independent times. f, Killing assays showing that the deletion of the Alg6 homologue in MACs (JF50_12690) dramatically impairs the killing effect against Sf9 insect cells. Shown are fLM images of Sf9 cells. Red (propidium iodide), dead cells; green (fluorescence diacetate), live cells; buffer, control (no MACs added). Scale bars, 50 μm. This experiment was performed three independent times with biological replicates.