9EON

270A Vipp1 dL10Ala helical tubes in the presence of EPL

9EON の概要

• エントリーDOI: 10.2210/pdb9eon/pdb
• EMDBエントリー: 19864
• 分子名称: Membrane-associated protein Vipp1 (1 entity in total)
• 機能のキーワード: membrane remodeling, membrane tubulation, lipid binding protein
• 由来する生物種: Synechocystis sp. PCC 6803
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29857.44

構造登録者

Junglas, B.,Sachse, C. (登録日: 2024-03-15, 公開日: 2024-10-16, 最終更新日: 2025-07-09)

主引用文献

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., 32:555-570, 2025

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: 39379528
DOI: 10.1038/s41594-024-01399-z

実験手法

ELECTRON MICROSCOPY (6.4 Å)