7F6V

Cryo-EM structure of the human TACAN channel in a closed state

Summary for 7F6V

• Entry DOI: 10.2210/pdb7f6v/pdb
• EMDB information: 31482
• Descriptor: Ion channel TACAN, CHOLESTEROL (2 entities in total)
• Functional Keywords: dimer, membrane protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 82087.62

Authors

Chen, X.Z.,Wang, Y.J.,Li, Y.,Yang, X.,Shen, Y.Q. (deposition date: 2021-06-25, release date: 2022-02-16, Last modification date: 2024-06-12)

Primary citation

Chen, X.,Wang, Y.,Li, Y.,Lu, X.,Chen, J.,Li, M.,Wen, T.,Liu, N.,Chang, S.,Zhang, X.,Yang, X.,Shen, Y.
Cryo-EM structure of the human TACAN in a closed state.
Cell Rep, 38:110445-110445, 2022

PubMed Abstract: TACAN is an ion channel-like protein that may be involved in sensing mechanical pain. Here, we present the cryo-electron microscopic structure of human TACAN (hTACAN). hTACAN forms a dimer in which each protomer consists of a transmembrane globular domain (TMD) containing six helices and an intracellular domain (ICD) containing two helices. Molecular dynamic simulations suggest that each protomer contains a putative ion conduction pore. A single-point mutation of the key residue Met207 greatly increases membrane pressure-activated currents. In addition, each hTACAN subunit binds one cholesterol molecule. Our data show the molecular assembly of hTACAN and suggest that wild-type hTACAN is in a closed state.

PubMed: 35235791
DOI: 10.1016/j.celrep.2022.110445

Experimental method

ELECTRON MICROSCOPY (3.66 Å)