7N7P

Cryo-EM structure of human TMEM120A

Summary for 7N7P

• Entry DOI: 10.2210/pdb7n7p/pdb
• EMDB information: 24230
• Descriptor: Ion channel TACAN, COENZYME A (2 entities in total)
• Functional Keywords: transmembrane protein, membrane protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 85561.98

Authors

Xue, J.,Han, Y.,Jiang, Y. (deposition date: 2021-06-10, release date: 2021-09-01, Last modification date: 2024-06-05)

Primary citation

Xue, J.,Han, Y.,Baniasadi, H.,Zeng, W.,Pei, J.,Grishin, N.V.,Wang, J.,Tu, B.P.,Jiang, Y.
TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty acid elongase.
Elife, 10:-, 2021

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 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.

PubMed: 34374645
DOI: 10.7554/eLife.71220

Experimental method

ELECTRON MICROSCOPY (3.24 Å)