3JAC: Cryo-em Study Of A Channel

Citation:
Abstract
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 A. 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.
PDB ID: 3JACDownload
MMDB ID: 132750
PDB Deposition Date: 2015/6/5
Updated in MMDB: 2015/11
Experimental Method:
electron microscopy
Resolution: 4.8  Å
Source Organism:
Similar Structures:
Biological Unit for 3JAC: trimeric; determined by author
Molecular Components in 3JAC
Label Count Molecule
Proteins (3 molecules)
3
Piezo-type Mechanosensitive Ion Channel Component 1(Gene symbol: Piezo1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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