Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1

Tatsuya Hagino, Takafumi Kato, Go Kasuya, Kan Kobayashi, Tsukasa Kusakizako, Shin Hamamoto, Tomoaki Sobajima, Yuichiro Fujiwara, Keitaro Yamashita, Hisashi Kawasaki, Andrés D. Maturana, Tomohiro Nishizawa () and Osamu Nureki ()
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Tatsuya Hagino: The University of Tokyo
Takafumi Kato: The University of Tokyo
Go Kasuya: Jichi Medical University
Kan Kobayashi: The University of Tokyo
Tsukasa Kusakizako: The University of Tokyo
Shin Hamamoto: The University of Tokyo
Tomoaki Sobajima: University of Oxford
Yuichiro Fujiwara: Kagawa University
Keitaro Yamashita: The University of Tokyo
Hisashi Kawasaki: The University of Tokyo
Andrés D. Maturana: Nagoya University
Tomohiro Nishizawa: The University of Tokyo
Osamu Nureki: The University of Tokyo

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: 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 Ca2+-gated anion channel. However, unlike bestrophin channels, VCCN1 lacks the Ca2+-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.

Date: 2022
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DOI: 10.1038/s41467-022-30292-w

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