7JI3

Cryo-EM structure of a proton-activated chloride channel

Summary for 7JI3

• Entry DOI: 10.2210/pdb7ji3/pdb
• EMDB information: 22343
• Descriptor: Proton-activated chloride channel (1 entity in total)
• Functional Keywords: ion channel, transport protein
• Biological source: Takifugu bimaculatus
• Total number of polymer chains: 3
• Total formula weight: 158722.92

Authors

Deng, Z.,Zhang, J.,Yuan, P. (deposition date: 2020-07-22, release date: 2021-03-03, Last modification date: 2024-11-06)

Primary citation

Deng, Z.,Zhao, Y.,Feng, J.,Zhang, J.,Zhao, H.,Rau, M.J.,Fitzpatrick, J.A.J.,Hu, H.,Yuan, P.
Cryo-EM structure of a proton-activated chloride channel TMEM206.
Sci Adv, 7:-, 2021

PubMed Abstract: TMEM206 has been recently identified as an evolutionarily conserved chloride channel that underlies ubiquitously expressed, proton-activated, outwardly rectifying anion currents. Here, we report the cryo-electron microscopy structure of pufferfish TMEM206, which forms a trimeric channel, with each subunit comprising two transmembrane segments and a large extracellular domain. An ample vestibule in the extracellular region is accessible laterally from the three side portals. The central pore contains multiple constrictions. A conserved lysine residue near the cytoplasmic end of the inner helix forms the presumed chloride ion selectivity filter. Unprecedentedly, the core structure and assembly closely resemble those of the epithelial sodium channel/degenerin family of sodium channels that are unrelated in amino acid sequence and conduct cations instead of anions. Together with electrophysiology, this work provides insights into ion conduction and gating for a new class of chloride channels that is architecturally distinct from previously characterized chloride channel families.

PubMed: 33627432
DOI: 10.1126/sciadv.abe5983

Experimental method

ELECTRON MICROSCOPY (3.46 Å)