7O40

Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity

7O40 の概要

• エントリーDOI: 10.2210/pdb7o40/pdb
• 関連するPDBエントリー: 7O3W 7O3X 7O3Y 7O3Z
• EMDBエントリー: 12710 12711 12712 12713 12714
• 分子名称: Protein sll0617, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: escrt-iii, membrane remodelling, nucleotide hydrolysis, photosynthesis, thylakoid biogenesis, stress response, lipid binding protein
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 173360.07

構造登録者

Gupta, T.K.,Klumpe, S.,Gries, K.,Strauss, M.,Rudack, T.,Schuller, J.M.,Schroda, M.,Engel, B.D. (登録日: 2021-04-03, 公開日: 2021-06-30, 最終更新日: 2024-07-10)

主引用文献

Gupta, T.K.,Klumpe, S.,Gries, K.,Heinz, S.,Wietrzynski, W.,Ohnishi, N.,Niemeyer, J.,Spaniol, B.,Schaffer, M.,Rast, A.,Ostermeier, M.,Strauss, M.,Plitzko, J.M.,Baumeister, W.,Rudack, T.,Sakamoto, W.,Nickelsen, J.,Schuller, J.M.,Schroda, M.,Engel, B.D.
Structural basis for VIPP1 oligomerization and maintenance of thylakoid membrane integrity.
Cell, 184:3643-, 2021

PubMed Abstract: Vesicle-inducing protein in plastids 1 (VIPP1) is essential for the biogenesis and maintenance of thylakoid membranes, which transform light into life. However, it is unknown how VIPP1 performs its vital membrane-remodeling functions. Here, we use cryo-electron microscopy to determine structures of cyanobacterial VIPP1 rings, revealing how VIPP1 monomers flex and interweave to form basket-like assemblies of different symmetries. Three VIPP1 monomers together coordinate a non-canonical nucleotide binding pocket on one end of the ring. Inside the ring's lumen, amphipathic helices from each monomer align to form large hydrophobic columns, enabling VIPP1 to bind and curve membranes. In vivo mutations in these hydrophobic surfaces cause extreme thylakoid swelling under high light, indicating an essential role of VIPP1 lipid binding in resisting stress-induced damage. Using cryo-correlative light and electron microscopy (cryo-CLEM), we observe oligomeric VIPP1 coats encapsulating membrane tubules within the Chlamydomonas chloroplast. Our work provides a structural foundation for understanding how VIPP1 directs thylakoid biogenesis and maintenance.

PubMed: 34166613
DOI: 10.1016/j.cell.2021.05.011

実験手法

ELECTRON MICROSCOPY (4.3 Å)