In the extremely selective fluoride channels from the bacterial Fluc family, fluoride ions access the pore via two points, an electropositive vestibule and a triad of conserved residues involved in anion recognition.
Single-particle cryo-EM and electrophysiology studies of the chloride channel TMEM16A reveals the structural basis for anion conduction and uncover its relationship to lipid scramblases of the same family.
Ion conduction in the calcium-activated chloride channel TMEM16A is directly regulated by calcium, which binds to a site close to the pore thereby shaping the electrostatics at its intracellular entrance.
Cryo-EM structures of the gating cycle of bestrophin reveal the molecular underpinnings of activation and inactivation gating in this calcium-activated chloride channel and reveal a surprisingly wide pore.
Substrate-induced structural changes in GtACR1 provide new insight into the chemical mechanism of natural light-gated anion conductance and facilitate its optimization for photoinhibition of neuron firing in optogenetics.