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TitleStructural basis for anion conduction in the calcium-activated chloride channel TMEM16A.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateMay 31, 2017
AuthorsCristina Paulino / Yvonne Neldner / Andy Km Lam / Valeria Kalienkova / Janine Denise Brunner / Stephan Schenck / Raimund Dutzler /
PubMed AbstractThe 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 ...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.
External linksElife / PubMed:28561733 / PubMed Central
MethodsEM (single particle)
Resolution6.6 Å
Structure data

3658

5nl2

EMDB-3658, PDB-5nl2:
cryo-EM structure of the mTMEM16A ion channel at 6.6 A resolution.
Method: EM (single particle) / Resolution: 6.6 Å

Source
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / TMEM16 family / ion channel / cryo-EM

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