7n7p
Cryo-EM structure of human TMEM120A
Structural highlights
FunctionTACAN_HUMAN Ion channel involved in sensing mechanical pain. Contributes to mechanosensitive currents in nocireceptors and detecting mechanical pain stimuli (By similarity). May also be required for efficient adipogenesis (PubMed:26024229).[UniProtKB:Q8C1E7][1] Publication Abstract from PubMedTMEM120A, also named as TACAN, is a novel membrane protein highly conserved in vertebrates and was recently proposed to be a mechanosensitive channel involved in sensing mechanical pain. Here we present the single-particle cryogenic electron microscopy (cryo-EM) structure of human TMEM120A, which forms a tightly packed dimer with extensive interactions mediated by the N-terminal coiled coil domain (CCD), the C-terminal transmembrane domain (TMD), and the re-entrant loop between the two domains. The TMD of each TMEM120A subunit contains six transmembrane helices (TMs) and has no clear structural feature of a channel protein. Instead, the six TMs form an alpha-barrel with a deep pocket where a coenzyme A (CoA) molecule is bound. Intriguingly, some structural features of TMEM120A resemble those of elongase for very long-chain fatty acids (ELOVL) despite the low sequence homology between them, pointing to the possibility that TMEM120A may function as an enzyme for fatty acid metabolism, rather than a mechanosensitive channel. TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty acid elongase.,Xue J, Han Y, Baniasadi H, Zeng W, Pei J, Grishin NV, Wang J, Tu BP, Jiang Y Elife. 2021 Aug 10;10:e71220. doi: 10.7554/eLife.71220. PMID:34374645[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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