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TitleArchitecture of the mammalian mechanosensitive Piezo1 channel.
Journal, issue, pagesNature, Vol. 527, Issue 7576, Page 64-69, Year 2015
Publish dateNov 5, 2015
AuthorsJingpeng Ge / Wanqiu Li / Qiancheng Zhao / Ningning Li / Maofei Chen / Peng Zhi / Ruochong Li / Ning Gao / Bailong Xiao / Maojun Yang /
PubMed AbstractPiezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have ...Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 Å. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore.
External linksNature / PubMed:26390154
MethodsEM (single particle) / X-ray diffraction
Resolution1.45 - 4.8 Å
Structure data

6343

3jac

EMDB-6343, PDB-3jac:
Cryo-EM study of a channel
Method: EM (single particle) / Resolution: 4.8 Å

PDB-4rax:
A regulatory domain of an ion channel
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsMETAL TRANSPORT / Cryo-EM / single particle / STRUCTURAL PROTEIN / sandwich fold / novel structure / extra-cellular / regulatory domain / regulatory

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