4RAX

A regulatory domain of an ion channel

Summary for 4RAX

• Entry DOI: 10.2210/pdb4rax/pdb
• Descriptor: Piezo-type mechanosensitive ion channel component 1 (2 entities in total)
• Functional Keywords: sandwich fold, novel structure, extra-cellular, regulatory domain, regulatory, structural protein
• Biological source: Mus musculus (mouse)
• Cellular location: Endoplasmic reticulum membrane ; Multi-pass membrane protein: E2JF22
• Total number of polymer chains: 1
• Total formula weight: 28346.79

Authors

Ge, J.,Yang, M. (deposition date: 2014-09-11, release date: 2015-09-23, Last modification date: 2018-04-18)

Primary citation

Ge, J.,Li, W.,Zhao, Q.,Li, N.,Chen, M.,Zhi, P.,Li, R.,Gao, N.,Xiao, B.,Yang, M.
Architecture of the mammalian mechanosensitive Piezo1 channel.
Nature, 527:64-69, 2015

PubMed 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 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.

PubMed: 26390154
DOI: 10.1038/nature15247

Experimental method

X-RAY DIFFRACTION (1.45 Å)