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| Hauptseite > Publikationsdatenbank > Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies |
| Hauptseite > Publikationsdatenbank > Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies |
| Journal Article | FZJ-2024-05814 |
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2025
Nature Publishing Group
London [u.a.]
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Please use a persistent id in citations: doi:10.1038/s41594-024-01399-z doi:10.34734/FZJ-2024-05814
Abstract: Vesicle-inducing protein in plastids 1 (Vipp1) is critical for thylakoid membrane biogenesis and maintenance. Although Vipp1 has recently been identified as a member of the endosomal sorting complexes required for transport III superfamily, it is still unknown how Vipp1 remodels membranes. Here, we present cryo-electron microscopy structures of Synechocystis Vipp1 interacting with membranes: seven structures of helical and stacked-ring assemblies at 5-7-Å resolution engulfing membranes and three carpet structures covering lipid vesicles at ~20-Å resolution using subtomogram averaging. By analyzing ten structures of N-terminally truncated Vipp1, we show that helix α0 is essential for membrane tubulation and forms the membrane-anchoring domain of Vipp1. Lastly, using a conformation-restrained Vipp1 mutant, we reduced the structural plasticity of Vipp1 and determined two structures of Vipp1 at 3.0-Å resolution, resolving the molecular details of membrane-anchoring and intersubunit contacts of helix α0. Our data reveal membrane curvature-dependent structural transitions from carpets to rings and rods, some of which are capable of inducing and/or stabilizing high local membrane curvature triggering membrane fusion.
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