{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["32(3)"],"submitter":["Junglas B"],"pubmed_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-restraine"],"journal":["Nature structural & molecular biology"],"pagination":["555-570"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11919686"],"repository":["biostudies-literature"],"pubmed_title":["Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies."],"pmcid":["PMC11919686"],"pubmed_authors":["Schneider D","Sachse C","Kartte D","Junglas B","Kutzner M","Hellmann N","Ritter I"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.","description":"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-restraine","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-06-01T15:09:32.995Z","creation":"2025-04-06T11:39:10.044Z"},"accession":"S-EPMC11919686","cross_references":{"pubmed":["39379528"],"doi":["10.1038/s41594-024-01399-z"]}}