8WUA
cryo-EM structure of human TMEM63A
Summary for 8WUA
| Entry DOI | 10.2210/pdb8wua/pdb |
| EMDB information | 37852 |
| Descriptor | CSC1-like protein 1 (1 entity in total) |
| Functional Keywords | mechanically activated (ma) ion channel, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 82331.83 |
| Authors | Yang, D. (deposition date: 2023-10-20, release date: 2024-01-24, Last modification date: 2025-07-02) |
| Primary citation | Wu, X.,Shang, T.,Lu, X.,Luo, D.,Yang, D. A monomeric structure of human TMEM63A protein. Proteins, 92:750-756, 2024 Cited by PubMed Abstract: OSCA/TMEM63 is a newly identified family of mechanically activated (MA) ion channels in plants and animals, respectively, which convert physical forces into electrical signals or trigger intracellular cascades and are essential for eukaryotic physiology. OSCAs and related TMEM16s and transmembrane channel-like (TMC) proteins form homodimers with two pores. However, the molecular architecture of the mammalian TMEM63 proteins remains unclear. Here we elucidate the structure of human TMEM63A in the presence of calcium by single particle cryo-EM, revealing a distinct monomeric architecture containing eleven transmembrane helices. It has structural similarity to the single subunit of the Arabidopsis thaliana OSCA proteins. We locate the ion permeation pathway within the monomeric configuration and observe a nonprotein density resembling lipid. These results lay a foundation for understanding the structural organization of OSCA/TMEM63A family proteins. PubMed: 38217391DOI: 10.1002/prot.26660 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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