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| 001 | 1031787 | ||
| 005 | 20250414120458.0 | ||
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| 100 | 1 | _ | |a Junglas, Benedikt |0 P:(DE-Juel1)181012 |b 0 |
| 245 | _ | _ | |a Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies |
| 260 | _ | _ | |a London [u.a.] |c 2025 |b Nature Publishing Group |
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| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Hellmann, Nadja |0 0000-0002-6591-8926 |b 3 |
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| 700 | 1 | _ | |a Schneider, Dirk |0 0000-0003-4517-6387 |b 5 |
| 700 | 1 | _ | |a Sachse, Carsten |0 P:(DE-Juel1)173949 |b 6 |e Corresponding author |
| 773 | _ | _ | |a 10.1038/s41594-024-01399-z |0 PERI:(DE-600)2131437-8 |p 555–570 |t Nature structural & molecular biology |v 32 |y 2025 |x 1545-9993 |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/1031787/files/s41594-024-01399-z.pdf |y OpenAccess |
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