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| Title | Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies. |
|---|---|
| Journal, issue, pages | Nat Struct Mol Biol, Year 2024 |
| Publish date | Oct 8, 2024 |
 Authors | Benedikt Junglas / David Kartte / Mirka Kutzner / Nadja Hellmann / Ilona Ritter / Dirk Schneider / Carsten Sachse /  |
| 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 ...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. |
 External links | Nat Struct Mol Biol / PubMed:39379528 |
| Methods | EM (helical sym.) / EM (single particle) / EM (subtomogram averaging) |
| Resolution | 3.0 - 18.0 Å |
| Structure data | EMDB-18384, PDB-8qfv: EMDB-18420, PDB-8qhv: EMDB-18421, PDB-8qhw:  EMDB-18422: C11 Vipp1 stacked rings in the presence of EPL  EMDB-18423: C12 Vipp1 stacked rings in the presence of EPL  EMDB-18424: C13 Vipp1 stacked rings in the presence of EPL  EMDB-18425: C14 Vipp1 stacked rings in the presence of EPL EMDB-18426, PDB-8qhx: EMDB-18427, PDB-8qhy: EMDB-18428, PDB-8qhz: EMDB-18429, PDB-8qi0: EMDB-18430, PDB-8qi1: EMDB-18431, PDB-8qi2: EMDB-18432, PDB-8qi3: EMDB-18433, PDB-8qi4: EMDB-18434, PDB-8qi5: EMDB-18435, PDB-8qi6:  EMDB-18620: Structure of Vipp1 carpet on EPL membrane EMDB-19863, PDB-9eom: EMDB-19864, PDB-9eon: EMDB-19865, PDB-9eoo: EMDB-19866, PDB-9eop:  EMDB-19899: C15 Vipp1 dL10Ala ring  EMDB-19900: C16 Vipp1 dL10Ala ring  EMDB-19901: C17 Vipp1 dL10Ala ring  EMDB-19902: C18 Vipp1 dL10Ala ring  EMDB-19903: C19 Vipp1 dL10Ala ring  EMDB-19904: C20 Vipp1 dL10Ala ring |
| Source |
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 Keywords | LIPID BINDING PROTEIN / membrane remodeling / membrane tubulation |
synechocystis sp. pcc 6803 (bacteria)