biostudies-literatureUnknown32(3)Junglas BVesicle-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-restraineNature structural & molecular biology555-570https://www.ebi.ac.uk/biostudies/studies/S-EPMC11919686biostudies-literatureStructural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.PMC11919686Schneider DSachse CKartte DJunglas BKutzner MHellmann NRitter IfalseStructural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.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-restraine2025-01-01T00:00:00Z2025 Mar2026-06-01T15:09:32.995Z2025-04-06T11:39:10.044ZS-EPMC119196863937952810.1038/s41594-024-01399-z