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001031787 1001_ $$0P:(DE-Juel1)181012$$aJunglas, Benedikt$$b0
001031787 245__ $$aStructural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies
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001031787 520__ $$aVesicle-inducing protein in plastids 1 (Vipp1) is critical for thylakoid membrane biogenesis and maintenance. Although Vipp1 has recently been identified as a member of the endosomal sorting complexes required for transport III superfamily, it is still unknown how Vipp1 remodels membranes. Here, we present cryo-electron microscopy structures of Synechocystis Vipp1 interacting with membranes: seven structures of helical and stacked-ring assemblies at 5-7-Å resolution engulfing membranes and three carpet structures covering lipid vesicles at ~20-Å resolution using subtomogram averaging. By analyzing ten structures of N-terminally truncated Vipp1, we show that helix α0 is essential for membrane tubulation and forms the membrane-anchoring domain of Vipp1. Lastly, using a conformation-restrained Vipp1 mutant, we reduced the structural plasticity of Vipp1 and determined two structures of Vipp1 at 3.0-Å resolution, resolving the molecular details of membrane-anchoring and intersubunit contacts of helix α0. Our data reveal membrane curvature-dependent structural transitions from carpets to rings and rods, some of which are capable of inducing and/or stabilizing high local membrane curvature triggering membrane fusion.
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001031787 7001_ $$0P:(DE-Juel1)191284$$aKartte, David$$b1$$ufzj
001031787 7001_ $$0P:(DE-HGF)0$$aKutzner, Mirka$$b2
001031787 7001_ $$00000-0002-6591-8926$$aHellmann, Nadja$$b3
001031787 7001_ $$0P:(DE-Juel1)131979$$aRitter, Ilona$$b4$$ufzj
001031787 7001_ $$00000-0003-4517-6387$$aSchneider, Dirk$$b5
001031787 7001_ $$0P:(DE-Juel1)173949$$aSachse, Carsten$$b6$$eCorresponding author
001031787 773__ $$0PERI:(DE-600)2131437-8$$a10.1038/s41594-024-01399-z$$p555–570$$tNature structural & molecular biology$$v32$$x1545-9993$$y2025
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