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- EMDB-7128: Structure of the mechanically activated ion channel Piezo1 -

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Basic information

Entry
Database: EMDB / ID: 7128
TitleStructure of the mechanically activated ion channel Piezo1
Map dataC3 symmetry refinement mouse Piezo1 core.
Samplemouse Piezo1
  • 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
Function/homologyPiezo 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
SourceMus musculus / House mouse / mammal /
MethodCryo EM / single particle reconstruction / 3.8 Å resolution
AuthorsSaotome K / Kefauver JM / Patapoutian A / Ward AB
CitationJournal: 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 ReportPDB-ID: 6bpz

SummaryFull reportAbout validation report
DateDeposition: Nov 27, 2017 / Header (metadata) release: Dec 27, 2017 / Map release: Dec 27, 2017 / Last update: Mar 7, 2018

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.032
  • Imaged by UCSF CHIMERA
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.032
  • Imaged by UCSF CHIMERA
  • Download
  • Surface view with fitted model
  • Atomic models: : PDB-6bpz
  • Surface level: 0.032
  • Imaged by UCSF CHIMERA
  • Download
3D viewer
Supplemental images

Downloads & links

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Map

Fileemd_7128.map.gz (map file in CCP4 format, 256001 KB)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
400 pix
1.03 Å/pix.
= 412. Å
400 pix
1.03 Å/pix.
= 412. Å
400 pix
1.03 Å/pix.
= 412. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider package.

Voxel sizeX=Y=Z: 1.03 Å
Density
Contour Level:0.032 (by author), 0.032 (movie #1):
Minimum - Maximum-0.07200906 - 0.13602789
Average (Standard dev.)3.5177873E-5 (0.0042542564)
Details

EMDB XML:

Space Group Number1
Map Geometry
Axis orderXYZ
Dimensions400400400
Origin000
Limit399399399
Spacing400400400
CellA=B=C: 412 Å
α=β=γ: 90 deg.

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.031.031.03
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z412.000412.000412.000
α/β/γ90.00090.00090.000
start NX/NY/NZ
NX/NY/NZ
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0720.1360.000

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Supplemental data

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Sample components

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Entire mouse Piezo1

EntireName: mouse Piezo1 / Number of components: 2
MassTheoretical: 876 kDa

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Component #1: protein, mouse Piezo1

ProteinName: mouse Piezo1 / Recombinant expression: No
MassTheoretical: 876 kDa
SourceSpecies: Mus musculus / House mouse / mammal /
Source (engineered)Expression System: Homo sapiens / / human / Cell of expression system: HEK293F

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Component #2: protein, Piezo-type mechanosensitive ion channel component 1,Piez...

ProteinName: 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
MassTheoretical: 161.973531 kDa
Source (engineered)Expression System: Mus musculus / House mouse / mammal /

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Experimental details

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Sample preparation

SpecimenSpecimen state: particle / Method: Cryo EM
Sample solutionSpecimen conc.: 5 mg/ml / pH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 60 e/Å2 / Illumination mode: FLOOD BEAM
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: FEI TITAN KRIOS AUTOGRID HOLDER
CameraDetector: GATAN K2 (4k x 4k)

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Image processing

ProcessingMethod: single particle reconstruction / Applied symmetry: C3 (3 fold cyclic) / Number of projections: 72627
3D reconstructionSoftware: RELION / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF

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Atomic model buiding

Output model

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