7EK2

Cryo-EM structure of VCCN1 in lipid nanodisc

7EK2 の概要

• エントリーDOI: 10.2210/pdb7ek2/pdb
• EMDBエントリー: 31166
• 分子名称: Bestrophin-like protein (1 entity in total)
• 機能のキーワード: ion channel, thylakoid, photosynthesis, bestrophin family, membrane protein
• 由来する生物種: Malus domestica (Apple, Pyrus malus)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42057.74

構造登録者

Hagino, T.,Kato, T.,Kasuya, G.,Kobayashi, K.,Kusakizako, T.,Yamashita, K.,Nishizawa, T.,Nureki, O. (登録日: 2021-04-03, 公開日: 2022-04-06, 最終更新日: 2024-06-05)

主引用文献

Hagino, T.,Kato, T.,Kasuya, G.,Kobayashi, K.,Kusakizako, T.,Hamamoto, S.,Sobajima, T.,Fujiwara, Y.,Yamashita, K.,Kawasaki, H.,Maturana, A.D.,Nishizawa, T.,Nureki, O.
Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1.
Nat Commun, 13:2505-2505, 2022

PubMed Abstract: In the light reaction of plant photosynthesis, modulation of electron transport chain reactions is important to maintain the efficiency of photosynthesis under a broad range of light intensities. VCCN1 was recently identified as a voltage-gated chloride channel residing in the thylakoid membrane, where it plays a key role in photoreaction tuning to avoid the generation of reactive oxygen species (ROS). Here, we present the cryo-EM structures of Malus domestica VCCN1 (MdVCCN1) in nanodiscs and detergent at 2.7 Å and 3.0 Å resolutions, respectively, and the structure-based electrophysiological analyses. VCCN1 structurally resembles its animal homolog, bestrophin, a Ca-gated anion channel. However, unlike bestrophin channels, VCCN1 lacks the Ca-binding motif but instead contains an N-terminal charged helix that is anchored to the lipid membrane through an additional amphipathic helix. Electrophysiological experiments demonstrate that these structural elements are essential for the channel activity, thus revealing the distinct activation mechanism of VCCN1.

PubMed: 35523970
DOI: 10.1038/s41467-022-30292-w

実験手法

ELECTRON MICROSCOPY (2.7 Å)