7CH1

The overall structure of SLC26A9

Summary for 7CH1

• Entry DOI: 10.2210/pdb7ch1/pdb
• EMDB information: 30368
• Descriptor: Solute carrier family 26 member 9, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: membrane protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 174321.68

Authors

Chi, X.M.,Chen, Y.,Li, X.R.,Zhang, Y.Y.,Zhou, Q. (deposition date: 2020-07-03, release date: 2020-08-26, Last modification date: 2024-03-27)

Primary citation

Chi, X.,Jin, X.,Chen, Y.,Lu, X.,Tu, X.,Li, X.,Zhang, Y.,Lei, J.,Huang, J.,Huang, Z.,Zhou, Q.,Pan, X.
Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence.
Cell Discov, 6:55-55, 2020

PubMed Abstract: The human SLC26 transporter family exhibits various transport characteristics, and family member SLC26A9 performs multiple roles, including acting as Cl/HCO exchangers, Cl channels, and Na transporters. Some mutations of SLC26A9 are correlated with abnormalities in respiration and digestion systems. As a potential target colocalizing with CFTR in cystic fibrosis patients, SLC26A9 is of great value in drug development. Here, we present a cryo-EM structure of the human SLC26A9 dimer at 2.6 Å resolution. A segment at the C-terminal end is bound to the entry of the intracellular vestibule of the putative transport pathway, which has been proven by electrophysiological experiments to be a gating modulator. Multiple chloride and sodium ions are resolved in the high-resolution structure, identifying novel ion-binding pockets for the first time. Together, our structure takes important steps in elucidating the structural features and regulatory mechanism of SLC26A9, with potential significance in the treatment of cystic fibrosis.

PubMed: 32818062
DOI: 10.1038/s41421-020-00193-7

Experimental method

ELECTRON MICROSCOPY (2.6 Å)