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TitleA monomeric structure of human TMEM63A protein.
Journal, issue, pagesProteins, Vol. 92, Issue 6, Page 750-756, Year 2024
Publish dateJan 13, 2024
AuthorsXuening Wu / Tiantian Shang / Xinyi Lü / Deyi Luo / Dongxue Yang /
PubMed AbstractOSCA/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 ...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.
External linksProteins / PubMed:38217391
MethodsEM (single particle)
Resolution3.6 Å
Structure data

37852

8wua

EMDB-37852, PDB-8wua:
cryo-EM structure of human TMEM63A
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / mechanically activated (MA) ion channel

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