7EK3
Cryo-EM structure of VCCN1 Y332A mutant in lipid nanodisc
Summary for 7EK3
| Entry DOI | 10.2210/pdb7ek3/pdb |
| EMDB information | 31167 |
| Descriptor | Bestrophin-like protein (1 entity in total) |
| Functional Keywords | ion channel, thylakoid, photosynthesis, bestrophin family, membrane protein |
| Biological source | Malus domestica (Apple, Pyrus malus) |
| Total number of polymer chains | 1 |
| Total formula weight | 41965.64 |
| Authors | Hagino, T.,Kato, T.,Kasuya, G.,Kobayashi, K.,Kusakizako, T.,Yamashita, K.,Nishizawa, T.,Nureki, O. (deposition date: 2021-04-03, release date: 2022-04-06, Last modification date: 2024-06-05) |
| Primary citation | 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 Cited by 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: 35523970DOI: 10.1038/s41467-022-30292-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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