期刊
ELIFE
卷 10, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.71220
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资金
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences [R35GM140892, R35GM136370, GM127390]
- Welch Foundation [I-1578, I-1505]
- National Science Foundation [1955260]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1955260] Funding Source: National Science Foundation
TMEM120A, also known as TACAN, is a novel membrane protein highly conserved in vertebrates and has been proposed to function as an enzyme for fatty acid metabolism, rather than a mechanosensitive channel, based on the cryo-EM structure analysis presented in this study.
TMEM120A, 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 a-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.
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