ArticleNature communications2022
Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Proton motive force partitioning links energy and redox balance to photoprotection and carbon gain.Frontiers in plant science · 2026Review
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Chlorine Modulates Photosynthetic Efficiency, Chlorophyll Fluorescence in Tomato Leaves, and Carbohydrate Allocation in Developing Fruits.International journal of molecular sciences · 2025Article
- The chloroplast-located HKT transporter plays an important role in fertilization and development in Physcomitrium patens.The Plant journal : for cell and molecular biology · 2025Article
- Bestrophin-like protein 4 is involved in photosynthetic acclimation to light fluctuations in Chlamydomonas.Plant physiology · 2024Article
- Overview of Membrane Protein Sample Preparation for Single-Particle Cryo-Electron Microscopy Analysis.International journal of molecular sciences · 2023Review
- eGFP as an All-in-One Tag for Purification of Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
- D139N mutation of PsbP enhances the oxygen-evolving activity of photosystem II through stabilized binding of a chloride ion.PNAS nexus · 2022Article
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Authors and funding
13 authors at 8 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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
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