8QFV
305A Vipp1 helical tubes in the presence of EPL
Summary for 8QFV
| Entry DOI | 10.2210/pdb8qfv/pdb |
| EMDB information | 18384 |
| Descriptor | Protein sll0617 (1 entity in total) |
| Functional Keywords | membrane remodeling, membrane tubulation, lipid binding protein |
| Biological source | Synechocystis sp. PCC 6803 |
| Total number of polymer chains | 1 |
| Total formula weight | 29965.50 |
| Authors | Junglas, B.,Sachse, C. (deposition date: 2023-09-05, release date: 2024-09-11, Last modification date: 2024-10-23) |
| Primary citation | Junglas, B.,Kartte, D.,Kutzner, M.,Hellmann, N.,Ritter, I.,Schneider, D.,Sachse, C. Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies. Nat.Struct.Mol.Biol., 2024 Cited by 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-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. PubMed: 39379528DOI: 10.1038/s41594-024-01399-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.1 Å) |
Structure validation
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