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- EMDB-0946: Cryo-EM structure of the mouse Piezo1 isoform Piezo1.1 -

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Basic information

Entry
Database: EMDB / ID: EMD-0946
TitleCryo-EM structure of the mouse Piezo1 isoform Piezo1.1
Map data
Sample
  • Complex: homo-trimer of Piezo1.1
    • Protein or peptide: Piezo-type mechanosensitive ion channel component 1
KeywordsPiezo1.1 / Mechanogating / Mechanotransduction channel / MEMBRANE PROTEIN / isoform
Function / homology
Function and homology information


mechanosensitive monoatomic cation channel activity / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / mechanosensitive monoatomic ion channel activity / positive regulation of integrin activation / positive regulation of myotube differentiation / monoatomic cation transport / lamellipodium membrane / monoatomic cation channel activity / endoplasmic reticulum-Golgi intermediate compartment membrane ...mechanosensitive monoatomic cation channel activity / positive regulation of cell-cell adhesion mediated by integrin / detection of mechanical stimulus / mechanosensitive monoatomic ion channel activity / positive regulation of integrin activation / positive regulation of myotube differentiation / monoatomic cation transport / lamellipodium membrane / monoatomic cation channel activity / endoplasmic reticulum-Golgi intermediate compartment membrane / regulation of membrane potential / cellular response to mechanical stimulus / endoplasmic reticulum membrane / endoplasmic reticulum / identical protein binding / plasma membrane
Similarity search - Function
Piezo family / Piezo non-specific cation channel, R-Ras-binding domain / Piezo domain / Piezo non-specific cation channel, R-Ras-binding domain / Piezo
Similarity search - Domain/homology
Piezo-type mechanosensitive ion channel component 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.5 Å
AuthorsGeng J / Liu W / Zhou H / Zhang T / Wang L / Zhang M / Shen B / Li X / Xiao B
CitationJournal: Neuron / Year: 2020
Title: A Plug-and-Latch Mechanism for Gating the Mechanosensitive Piezo Channel.
Authors: Jie Geng / Wenhao Liu / Heng Zhou / Tingxin Zhang / Li Wang / Mingmin Zhang / Yiran Li / Bo Shen / Xueming Li / Bailong Xiao /
Abstract: The mechanosensitive Piezo1 and Piezo2 channels convert mechanical force into cation permeation. However, their precise mechanogating and regulatory mechanisms remain elusive. Here, we report that ...The mechanosensitive Piezo1 and Piezo2 channels convert mechanical force into cation permeation. However, their precise mechanogating and regulatory mechanisms remain elusive. Here, we report that Piezo1 utilizes three lateral ion-conducting portals equipped with physical gates for cooperative gating and splicing regulation. Mutating residues lining the portal converts Piezo1 into an anion-selective channel, demonstrating the portal-based cation-permeating pathway. Intriguingly, the portal is physically blocked with a plug domain, which undergoes alternative splicing in both Piezo1 and Piezo2. The Piezo1 isoform has local openings of the portals, enlarged single-channel conductance and sensitized mechanosensitivity. Remarkably, the three plugs are strategically latched onto the central axis for coordinated gating of the three portals. Disrupting the latching induces three quantal sub-conductance states in Piezo1, but not in the isoform. Together, we propose that Piezo utilizes an elegant plug-and-latch mechanism to physically and coordinately gate the lateral portals through the spliceable plug gates.
History
DepositionJan 13, 2020-
Header (metadata) releaseMar 4, 2020-
Map releaseMar 4, 2020-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6lqi
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0946.png

Downloads & links

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Map

FileDownload / File: emd_0946.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.32 Å
Density
Contour LevelBy AUTHOR: 0.015 / Movie #1: 0.015
Minimum - Maximum-0.04405964 - 0.078448065
Average (Standard dev.)0.00025988478 (±0.0022025246)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 369.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.321.321.32
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z369.600369.600369.600
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-0.0440.0780.000

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Supplemental data

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Sample components

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Entire : homo-trimer of Piezo1.1

EntireName: homo-trimer of Piezo1.1
Components
  • Complex: homo-trimer of Piezo1.1
    • Protein or peptide: Piezo-type mechanosensitive ion channel component 1

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Supramolecule #1: homo-trimer of Piezo1.1

SupramoleculeName: homo-trimer of Piezo1.1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 880 KDa

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Macromolecule #1: Piezo-type mechanosensitive ion channel component 1

MacromoleculeName: Piezo-type mechanosensitive ion channel component 1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 289.590625 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MEPHVLGAGL YWLLLPCTLL AASLLRFNAL SLVYLLFLLL LPWLPGPSRH SIPGHTGRLL RALLCLSLLF LVAHLAFQIC LHTVPHLDQ FLGQNGSLWV KVSQHIGVTR LDLKDIFNTT RLVAPDLGVL LASSLCLGLC GRLTRKAGQS RRTQELQDDD D DDDDDDED ...String:
MEPHVLGAGL YWLLLPCTLL AASLLRFNAL SLVYLLFLLL LPWLPGPSRH SIPGHTGRLL RALLCLSLLF LVAHLAFQIC LHTVPHLDQ FLGQNGSLWV KVSQHIGVTR LDLKDIFNTT RLVAPDLGVL LASSLCLGLC GRLTRKAGQS RRTQELQDDD D DDDDDDED IDAAPAVGLK GAPALATKRR LWLASRFRVT AHWLLMTSGR TLVIVLLALA GIAHPSAFSS IYLVVFLAIC TW WSCHFPL SPLGFNTLCV MVSCFGAGHL ICLYCYQTPF IQDMLPPGNI WARLFGLKNF VDLPNYSSPN ALVLNTKHAW PIY VSPGIL LLLYYTATSL LKLHKSCPSE LRKETPREDE EHELELDHLE PEPQARDATQ GEMPMTTEPD LDNCTVHVLT SQSP VRQRP VRPRLAELKE MSPLHGLGHL IMDQSYVCAL IAMMVWSIMY HSWLTFVLLL WACLIWTVRS RHQLAMLCSP CILLY GLTL CCLRYVWAME LPELPTTLGP VSLHQLGLEH TRYPCLDLGA MLLYLLTFWL LLRQFVKEKL LKKQKVPAAL LEVTVA DTE PTQTQTLLRS LGELVTGIYV KYWIYVCAGM FIVVSFAGRL VVYKIVYMFL FLLCLTLFQV YYTLWRKLLR VFWWLVV AY TMLVLIAVYT FQFQDFPTYW RNLTGFTDEQ LGDLGLEQFS VSELFSSILI PGFFLLACIL QLHYFHRPFM QLTDLEHV P PPGTRHPRWA HRQDAVSEAP LLEHQEEEEV FREDGQSMDG PHQATQVPEG TASKWGLVAD RLLDLAASFS AVLTRIQVF VRRLLELHVF KLVALYTVWV ALKEVSVMNL LLVVLWAFAL PYPRFRPMAS CLSTVWTCII IVCKMLYQLK IVNPHEYSSN CTEPFPNNT NLQPLEINQS LLYRGPVDPA NWFGVRKGYP NLGYIQNHLQ ILLLLVFEAV VYRRQEHYRR QHQQAPLPAQ A VCADGTRQ RLDQDLLSCL KYFINFFFYK FGLEICFLMA VNVIGQRMNF MVILHGCWLV AILTRRRREA IARLWPNYCL FL TLFLLYQ YLLCLGMPPA LCIDYPWRWS KAIPMNSALI KWLYLPDFFR APNSTNLISD FLLLLCASQQ WQVFSAERTE EWQ RMAGIN TDHLEPLRGE PNPIPNFIHC RSYLDMLKVA VFRYLFWLVL VVVFVAGATR ISIFGLGYLL ACFYLLLFGT TLLQ KDTRA QLVLWDCLIL YNVTVIISKN MLSLLSCVFV EQMQSNFCWV IQLFSLVCTV KGYYDPKEMM TRDRDCLLPV EEAGI IWDS ICFFFLLLQR RIFLSHYFLH VSADLKATAL QASRGFALYN AANLKSINFH RQIEEKSLAQ LKRQMKRIRA KQEKYR QSQ ASRGQLQSKD PQDPSQEPVI HSGDYFLFES DSEEEEEALP EDPRPAAQSA FQMAYQAWVT NAQTVLRQRR ERARQER AE QLASGGDLNP DVEPVDVPED EMAGRSHMMQ RVLSTMQFLW VLGQATVDGL TRWLRAFTKH HRTMSDVLCA ERYLLTQE L LRVGEVRRGV LDQLYVGEDE ATLSGPVETR DGPSTASSGL GAEEPLSSMT DDTSSPLSTG YNTRSGSEEI VTDAGDLQA GTSLHGSQEL LANARTRMRT ASELLLDRRL HIPELEEAER FEAQQGRTLR LLRAGYQCVA AHSELLCYFI IILNHMVTAS AASLVLPVL VFLWAMLTIP RPSKRFWMTA IVFTEVMVVT KYLFQFGFFP WNSYVVLRRY ENKPYFPPRI LGLEKTDSYI K YDLVQLMA LFFHRSQLLC YGLWDHEEDR YPKDHCRSSV KDREAKEEPE AKLESQSETG TGHPKEPVLA GTPRDHIQGK GS IRSKDVI QDPPEDLKPR HTRHISIRFR RRKETPGPKG TAVMETEHEE GEGKETTERK RPRHTQEKSK FRERMKAAGR RLQ SFCVSL AQSFYQPLQR FFHDILHTKY RAATDVYALM FLADIVDIII IIFGFWAFGK HSAATDIASS LSDDQVPQAF LFML LVQFG TMVIDRALYL RKTVLGKLAF QVVLVVAIHI WMFFILPAVT ERMFSQNAVA QLWYFVKCIY FALSAYQIRC GYPTR ILGN FLTKKYNHLN LFLFQGFRLV PFLVELRAVM DWVWTDTTLS LSNWMCVEDI YANIFIIKCS RETEKKYPQP KGQKKK KIV KYGMGGLIIL FLIAIIWFPL LFMSLIRSVV GVVNQPIDVT VTLKLGGYEP LFTMSAQQPS IVPFTPQAYE ELSQQFD PY PLAMQFISQY SPEDIVTAQI EGSSGALWRI SPPSRAQMKQ ELYNGTADIT LRFTWNFQRD LAKGGTVEYT NEKHTLEL A PNSTARRQLA QLLEGRPDQS VVIPHLFPKY IRAPNGPEAN PVKQLQPDEE EDYLGVRIQL RREQVGTGAS GEQAGTKAS DFLEWWVIEL QDCKADCNLL PMVIFSDKVS PPSLGFLAGY GIVGLYVSIV LVVGKFVRGF FSEISHSIMF EELPCVDRIL KLCQDIFLV RETRELELEE ELYAKLIFLY RSPETMIKWT RERE

UniProtKB: Piezo-type mechanosensitive ion channel component 1

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 281 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 179654
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-6lqi:
Cryo-EM structure of the mouse Piezo1 isoform Piezo1.1

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