5NL2

cryo-EM structure of the mTMEM16A ion channel at 6.6 A resolution.

Summary for 5NL2

• Entry DOI: 10.2210/pdb5nl2/pdb
• EMDB information: 3658
• Descriptor: Anoctamin-1 (1 entity in total)
• Functional Keywords: tmem16 family, ion channel, membrane protein, cryo-em
• Biological source: Mus musculus (Mouse)
• Cellular location: Cell membrane ; Multi-pass membrane protein : Q8BHY3
• Total number of polymer chains: 2
• Total formula weight: 222117.98

Authors

Paulino, C.,Neldner, Y.,Lam, K.M.,Kalienkova, V.,Brunner, J.D.,Schenck, S.,Dutzler, R. (deposition date: 2017-04-03, release date: 2017-06-07, Last modification date: 2024-05-15)

Primary citation

Paulino, C.,Neldner, Y.,Lam, A.K.,Kalienkova, V.,Brunner, J.D.,Schenck, S.,Dutzler, R.
Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A.
Elife, 6:-, 2017

PubMed Abstract: The calcium-activated chloride channel TMEM16A is a member of a conserved protein family that comprises ion channels and lipid scramblases. Although the structure of the scramblase nhTMEM16 has defined the architecture of the family, it was unknown how a channel has adapted to cope with its distinct functional properties. Here we have addressed this question by the structure determination of mouse TMEM16A by cryo-electron microscopy and a complementary functional characterization. The protein shows a similar organization to nhTMEM16, except for changes at the site of catalysis. There, the conformation of transmembrane helices constituting a membrane-spanning furrow that provides a path for lipids in scramblases has changed to form an enclosed aqueous pore that is largely shielded from the membrane. Our study thus reveals the structural basis of anion conduction in a TMEM16 channel and it defines the foundation for the diverse functional behavior in the TMEM16 family.

PubMed: 28561733
DOI: 10.7554/eLife.26232

Experimental method

ELECTRON MICROSCOPY (6.6 Å)