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- EMDB-74433: Low-resolution electron density map of C. elegans PEZO-1 Isoform L -

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Basic information

Entry
Database: EMDB / ID: EMD-74433
TitleLow-resolution electron density map of C. elegans PEZO-1 Isoform L
Map data
Sample
  • Complex: C. elegans PEZO-1 Isoform L
    • Protein or peptide: C. elegans PEZO-1 Isoform L
KeywordsPEZO-1 / Piezo / Mechanosensation / MEMBRANE PROTEIN
Biological speciesCaenorhabditis elegans (invertebrata)
Methodsingle particle reconstruction / cryo EM / Resolution: 8.1 Å
AuthorsBell B / Vasquez V
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35GM153208 United States
CitationJournal: Cell Rep / Year: 2026
Title: Structures of invertebrate PEZO-1 isoforms with a compact architecture and a dispensable pore-distal N-terminal blade.
Authors: Briar Bell / Angela M Jaramillo-Granada / Daniel J Orlin / Wei-Hsiang Weng / Haosheng Wen / Marcos Sotomayor / Alexander T Chesler / Matthew L Baker / Julio F Cordero-Morales / Valeria Vásquez /
Abstract: PIEZO channels are mechanosensitive ion channels conserved from plants to humans, yet structures exist for only a few mammalian orthologs. We define the structural and functional diversity of ...PIEZO channels are mechanosensitive ion channels conserved from plants to humans, yet structures exist for only a few mammalian orthologs. We define the structural and functional diversity of Caenorhabditis elegans PEZO-1, a single gene with extensive alternative splicing, by determining cryo-electron microscopy structures of three representative isoforms: G (full length), K (lacking the pore-distal N-terminal blade), and L (missing most of the blade). PEZO-1G displays mechanically evoked currents yet adopts a compact, semi-flattened conformation that significantly differs from the mammalian domes. The blades exhibit a three-step slope architecture stabilized by inter-blade latching among transmembrane helical units, yielding a circular, steering-wheel-like arrangement. A wider cap enables distinct blade-cap contacts that stabilize a "toggle-down" conformation. Isoform K also exhibits mechanically evoked currents, indicating that the pore-distal N-terminal blade is dispensable for mechanoactivation. Computational membrane-deformation modeling indicates that the isoforms impose distinct curvatures on the bilayer. Our findings indicate an evolutionarily distinct architecture for PEZO-1.
History
DepositionDec 12, 2025-
Header (metadata) releaseDec 24, 2025-
Map releaseDec 24, 2025-
UpdateJul 22, 2026-
Current statusJul 22, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_74433.png

Downloads & links

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Map

FileDownload / File: emd_74433.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 400 pix.
= 432. Å		1.08 Å/pix.
x 400 pix.
= 432. Å		1.08 Å/pix.
x 400 pix.
= 432. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0677
Minimum - Maximum-0.14985436 - 0.35854053
Average (Standard dev.)0.00012682987 (±0.010426695)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 432.00003 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_74433_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_74433_half_map_2.map
Projections & Slices
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Histogram

Histogram (log scale)

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Sample components

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Entire : C. elegans PEZO-1 Isoform L

EntireName: C. elegans PEZO-1 Isoform L
Components
  • Complex: C. elegans PEZO-1 Isoform L
    • Protein or peptide: C. elegans PEZO-1 Isoform L

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Supramolecule #1: C. elegans PEZO-1 Isoform L

SupramoleculeName: C. elegans PEZO-1 Isoform L / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Caenorhabditis elegans (invertebrata)

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Macromolecule #1: C. elegans PEZO-1 Isoform L

MacromoleculeName: C. elegans PEZO-1 Isoform L / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Caenorhabditis elegans (invertebrata)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MFKYDPENDD LVEPVDSFVP EVDPKATAYD RLDPGQIMYA ATAHDLDLAK TVQQVKKGDT IKDPDSRALI AVSEPEARKP GGTEETDGDE DEDNKDSKVE STAKFIQKMI ASALDLCSVT LNKLCREHRY VGFVLSKEKQ KLKSGHSESL SNTSRKLTDI RSAVDLPSLQ ...String:
MFKYDPENDD LVEPVDSFVP EVDPKATAYD RLDPGQIMYA ATAHDLDLAK TVQQVKKGDT IKDPDSRALI AVSEPEARKP GGTEETDGDE DEDNKDSKVE STAKFIQKMI ASALDLCSVT LNKLCREHRY VGFVLSKEKQ KLKSGHSESL SNTSRKLTDI RSAVDLPSLQ LVQSANDVEK METAVSVDWQ QKSSATRLLN AVVNCIGAHT DILCYFFAIM TQVMTGGLIT LPLPLMSLFW GNLSNPRPSK FFWVTMITYT ECVIVIKFVC QFAFMPYNSI TWRTEHQMDP MSLDKLFGVS QRDSFALWDI VLLFSLFFHR YMLRKLGLWK DANLTDTFTL KEEPRSASGS DTGSPKKIAQ EPKVVVTQSD TLEGTSGGEI VIPSDPNAVS NMEELDCEPP IPEKQSGPIG RFIHQLFHPK FRYIRDLYPI MFGIDVICFL IMTFGYSAFG EGGSGNVLDD VKASRIPVTL VVMLVGMTLA IIIDRALYLR KSVVGKLIYQ VLMIAFLHIW VFLVLPNMTR RSAISNHVAQ ALYVIKSCYF LVSAWQIRNG YPELCIGNLL THSYGMTNMI AFKVFMNIPF LFELRTAIDW TWTDTSMPLF DFFNMENFYA HIFNIKCARQ FEAAYPAPRG IPKGKLVKYM MGFPIIIGVV IFIFSPLLLW SLLNQIGTIS MPEKVTLRIS IEGYPPLYEM EAQGSNHDNA ELGMIKPDQL ASLNQALTDS YTTRDTNSIL RSRMSVSYLK GYTYEDILIV RFRPESEIYW PISQDSRNAM IDKLSRNTSV NFEVSLEFTR PYDPNENAAL KHSKSWLVPI SLDMTIRAKI QSALRGDPGH PILIPQSIPA FIQVPNQGEL TLPTSIGNTI INDGNPRINT TGMEKSDEAR AWFDSLTLNL EQGKSQNEKM WIATSEHPGD QNAKLWIKTA NTTYSGRPYL QVVGFIDRAF PSFLAKVFKG GVIAVYLSVI LVVGRGLVRG IFTTSPSTVM FTELPNADHL LKICLDIYLV REAKDFMLEQ DLFAKLIFLF RSPATLIEWT RMSKKKQE

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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: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / 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 / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 130000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionApplied symmetry - Point group: C3 (3 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 8.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 227008
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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