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-Structure paper
| Title | TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty acid elongase. |
|---|---|
| Journal, issue, pages | Elife, Vol. 10, Year 2021 |
| Publish date | Aug 10, 2021 |
Authors | Jing Xue / Yan Han / Hamid Baniasadi / Weizhong Zeng / Jimin Pei / Nick V Grishin / Junmei Wang / Benjamin P Tu / Youxing Jiang / ![]() |
| PubMed Abstract | 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 ...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 α-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. |
External links | Elife / PubMed:34374645 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.24 Å |
| Structure data | EMDB-24230, PDB-7n7p: |
| Chemicals | ![]() ChemComp-COA: |
| Source |
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Keywords | MEMBRANE PROTEIN / Transmembrane protein |
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homo sapiens (human)
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