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

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 inst

SUBMITTER: Hagino T 

PROVIDER: S-EPMC9076864 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature