8K0B

Cryo-EM structure of TMEM63C

Summary for 8K0B

• Entry DOI: 10.2210/pdb8k0b/pdb
• EMDB information: 36759
• Descriptor: Calcium permeable stress-gated cation channel 1 (1 entity in total)
• Functional Keywords: mechanosensitive ion channel, membrane protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 93111.83

Authors

Qin, Y.,Yu, D.,Dong, J.,Dang, S. (deposition date: 2023-07-08, release date: 2023-12-06, Last modification date: 2025-07-02)

Primary citation

Qin, Y.,Yu, D.,Wu, D.,Dong, J.,Li, W.T.,Ye, C.,Cheung, K.C.,Zhang, Y.,Xu, Y.,Wang, Y.,Shi, Y.S.,Dang, S.
Cryo-EM structure of TMEM63C suggests it functions as a monomer.
Nat Commun, 14:7265-7265, 2023

PubMed Abstract: The TMEM63 family proteins (A, B, and C), calcium-permeable channels in animals that are preferentially activated by hypo-osmolality, have been implicated in various physiological functions. Deficiency of these channels would cause many diseases including hearing loss. However, their structures and physiological roles are not yet well understood. In this study, we determine the cryo-electron microscopy (cryo-EM) structure of the mouse TMEM63C at 3.56 Å, and revealed structural differences compared to TMEM63A, TMEM63B, and the plant orthologues OSCAs. Further structural guided mutagenesis and calcium imaging demonstrated the important roles of the coupling of TM0 and TM6 in channel activity. Additionally, we confirm that TMEM63C exists primarily as a monomer under physiological conditions, in contrast, TMEM63B is a mix of monomer and dimer in cells, suggesting that oligomerization is a regulatory mechanism for TMEM63 proteins.

PubMed: 37945568
DOI: 10.1038/s41467-023-42956-2

Experimental method

ELECTRON MICROSCOPY (3.56 Å)