8wua
From Proteopedia
cryo-EM structure of human TMEM63A
Structural highlights
DiseaseCSCL1_HUMAN The disease is caused by variants affecting the gene represented in this entry. FunctionCSCL1_HUMAN Acts as an osmosensitive calcium-permeable cation channel (PubMed:30382938, PubMed:31587869). Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion (PubMed:30382938, PubMed:31587869, PubMed:37543036).[UniProtKB:Q91YT8][1] [2] [3] Publication Abstract from PubMedOSCA/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. A monomeric structure of human TMEM63A protein.,Wu X, Shang T, Lu X, Luo D, Yang D Proteins. 2024 Jun;92(6):750-756. doi: 10.1002/prot.26660. Epub 2024 Jan 13. PMID:38217391[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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