|Entry||Database: EMDB / ID: 7128|
|Title||Structure of the mechanically activated ion channel Piezo1|
|Map data||C3 symmetry refinement mouse Piezo1 core.|
|Function/homology||Piezo non-specific cation channel, R-Ras-binding domain / Piezo domain / Piezo family / |Piezo / Piezo non-specific cation channel, R-Ras-binding domain / mechanosensitive ion channel activity / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / positive regulation of integrin activation / cation channel activity ...Piezo non-specific cation channel, R-Ras-binding domain / Piezo domain / Piezo family / |Piezo / Piezo non-specific cation channel, R-Ras-binding domain / mechanosensitive ion channel activity / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / positive regulation of integrin activation / cation channel activity / cation transport / lamellipodium membrane / regulation of membrane potential / endoplasmic reticulum-Golgi intermediate compartment membrane / cellular response to mechanical stimulus / endoplasmic reticulum membrane / endoplasmic reticulum / integral component of membrane / identical protein binding / plasma membrane / Piezo-type mechanosensitive ion channel component 1|
Function and homology information
|Source||Mus musculus / House mouse / mammal /|
|Method||Cryo EM / single particle reconstruction / 3.8 Å resolution|
|Authors||Saotome K / Kefauver JM / Patapoutian A / Ward AB|
|Citation||Journal: Nature / Year: 2018|
Title: Structure of the mechanically activated ion channel Piezo1.
Authors: Kei Saotome / Swetha E Murthy / Jennifer M Kefauver / Tess Whitwam / Ardem Patapoutian / Andrew B Ward
Abstract: Piezo1 and Piezo2 are mechanically activated ion channels that mediate touch perception, proprioception and vascular development. Piezo proteins are distinct from other ion channels and their ...Piezo1 and Piezo2 are mechanically activated ion channels that mediate touch perception, proprioception and vascular development. Piezo proteins are distinct from other ion channels and their structure remains poorly defined, which impedes detailed study of their gating and ion permeation properties. Here we report a high-resolution cryo-electron microscopy structure of the mouse Piezo1 trimer. The detergent-solubilized complex adopts a three-bladed propeller shape with a curved transmembrane region containing at least 26 transmembrane helices per protomer. The flexible propeller blades can adopt distinct conformations, and consist of a series of four-transmembrane helical bundles that we term Piezo repeats. Carboxy-terminal domains line the central ion pore, and the channel is closed by constrictions in the cytosol. A kinked helical beam and anchor domain link the Piezo repeats to the pore, and are poised to control gating allosterically. The structure provides a foundation to dissect further how Piezo channels are regulated by mechanical force.
|Validation Report||PDB-ID: 6bpz|
SummaryFull reportAbout validation report
|Date||Deposition: Nov 27, 2017 / Header (metadata) release: Dec 27, 2017 / Map release: Dec 27, 2017 / Last update: Mar 7, 2018|
Downloads & links
|File||emd_7128.map.gz (map file in CCP4 format, 256001 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 1.03 Å|
CCP4 map header:
-Entire mouse Piezo1
|Entire||Name: mouse Piezo1 / Number of components: 2|
|Mass||Theoretical: 876 kDa|
-Component #1: protein, mouse Piezo1
|Protein||Name: mouse Piezo1 / Recombinant expression: No|
|Mass||Theoretical: 876 kDa|
|Source||Species: Mus musculus / House mouse / mammal /|
|Source (engineered)||Expression System: Homo sapiens / / human / Cell of expression system: HEK293F|
-Component #2: protein, Piezo-type mechanosensitive ion channel component 1,Piez...
|Protein||Name: Piezo-type mechanosensitive ion channel component 1,Piezo-type mechanosensitive ion channel component 1,mouse Piezo1,Piezo-type mechanosensitive ion channel component 1,Piezo-type mechanosensitive ion channel component 1|
Recombinant expression: No
|Mass||Theoretical: 161.973531 kDa|
|Source (engineered)||Expression System: Mus musculus / House mouse / mammal /|
|Specimen||Specimen state: particle / Method: Cryo EM|
|Sample solution||Specimen conc.: 5 mg/ml / pH: 8|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 60 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C3 (3 fold cyclic) / Number of projections: 72627|
|3D reconstruction||Software: RELION / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF|
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