7N0L

Cryo-EM structure of TACAN in the H196A H197A mutant form (TMEM120A)

Summary for 7N0L

• Entry DOI: 10.2210/pdb7n0l/pdb
• Related: 7N0K
• EMDB information: 24107 24108
• Descriptor: Ion channel TACAN, COENZYME A (2 entities in total)
• Functional Keywords: lipid metabolism, coenzyme a, membrane protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 82861.39

Authors

Niu, Y.,Tao, X.,MacKinnon, R. (deposition date: 2021-05-25, release date: 2021-09-15, Last modification date: 2024-05-29)

Primary citation

Niu, Y.,Tao, X.,Vaisey, G.,Olinares, P.D.B.,Alwaseem, H.,Chait, B.T.,MacKinnon, R.
Analysis of the mechanosensor channel functionality of TACAN.
Elife, 10:-, 2021

PubMed Abstract: Mechanosensitive ion channels mediate transmembrane ion currents activated by mechanical forces. A mechanosensitive ion channel called TACAN was recently reported. We began to study TACAN with the intent to understand how it senses mechanical forces and functions as an ion channel. Using cellular patch-recording methods, we failed to identify mechanosensitive ion channel activity. Using membrane reconstitution methods, we found that TACAN, at high protein concentrations, produces heterogeneous conduction levels that are not mechanosensitive and are most consistent with disruptions of the lipid bilayer. We determined the structure of TACAN using single-particle cryo-electron microscopy and observed that it is a symmetrical dimeric transmembrane protein. Each protomer contains an intracellular-facing cleft with a coenzyme A cofactor, confirmed by mass spectrometry. The TACAN protomer is related in three-dimensional structure to a fatty acid elongase, ELOVL7. Whilst its physiological function remains unclear, we anticipate that TACAN is not a mechanosensitive ion channel.

PubMed: 34374644
DOI: 10.7554/eLife.71188

Experimental method

ELECTRON MICROSCOPY (2.8 Å)