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- EMDB-47073: Membrane-spanning OlyA/PlyB pore complex -

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Basic information

Entry
Database: EMDB / ID: EMD-47073
TitleMembrane-spanning OlyA/PlyB pore complex
Map dataMembrane-spanning OlyA/PlyB pore complex
Sample
  • Complex: Membrane-spanning OlyA/PlyB pore complex
    • Protein or peptide: Pleurotolysin B
    • Protein or peptide: Ostreolysin A6
Keywordsmembrane / pore formation / lipid interaction / MEMBRANE PROTEIN
Function / homology
Function and homology information


symbiont-mediated hemolysis of host erythrocyte
Similarity search - Function
Pleurotolysin B, C-terminal / : / Pleurotolysin B C-terminal domain / Fungal MACPF-like domain / Hemolysin, aegerolysin type / Aegerolysin / Membrane attack complex/perforin (MACPF) domain profile. / Membrane attack complex component/perforin (MACPF) domain
Similarity search - Domain/homology
Ostreolysin A6 / Pleurotolysin B
Similarity search - Component
Biological speciesPleurotus ostreatus (oyster mushroom)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.47 Å
AuthorsSmothers J / Chen Z / Li Y / Han Y / Radhakrishnan A
Funding support United States, France, 5 items
OrganizationGrant numberCountry
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)HL160487 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI158357 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)T32GM131963 United States
Welch FoundationI-1793 United States
Leducq Foundation19CVD04 France
CitationJournal: To Be Published
Title: Membrane-spanning OlyA/PlyB pore complex
Authors: Smothers J / Chen Z / Li Y / Han Y / Radhakrishnan A
History
DepositionSep 18, 2024-
Header (metadata) releaseSep 24, 2025-
Map releaseSep 24, 2025-
UpdateSep 24, 2025-
Current statusSep 24, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_47073.png

Downloads & links

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Map

FileDownload / File: emd_47073.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMembrane-spanning OlyA/PlyB pore complex
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 512 pix.
= 424.96 Å		0.83 Å/pix.
x 512 pix.
= 424.96 Å		0.83 Å/pix.
x 512 pix.
= 424.96 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.83 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.075
Minimum - Maximum-0.21935883 - 0.64121014
Average (Standard dev.)0.0013021562 (±0.016376076)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 424.96 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Membrane-spanning OlyA/PlyB pore complex half map 1

Fileemd_47073_half_map_1.map
AnnotationMembrane-spanning OlyA/PlyB pore complex half map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Membrane-spanning OlyA/PlyB pore complex half map 2

Fileemd_47073_half_map_2.map
AnnotationMembrane-spanning OlyA/PlyB pore complex half map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Membrane-spanning OlyA/PlyB pore complex

EntireName: Membrane-spanning OlyA/PlyB pore complex
Components
  • Complex: Membrane-spanning OlyA/PlyB pore complex
    • Protein or peptide: Pleurotolysin B
    • Protein or peptide: Ostreolysin A6

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Supramolecule #1: Membrane-spanning OlyA/PlyB pore complex

SupramoleculeName: Membrane-spanning OlyA/PlyB pore complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Pleurotus ostreatus (oyster mushroom)
Molecular weightTheoretical: 1.2 MDa

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Macromolecule #1: Pleurotolysin B

MacromoleculeName: Pleurotolysin B / type: protein_or_peptide / ID: 1 / Number of copies: 13 / Enantiomer: LEVO
Source (natural)Organism: Pleurotus ostreatus (oyster mushroom)
Molecular weightTheoretical: 53.244539 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString: HHHHHHHHSQ AGDTLNDVIQ DPTRRNKLIN DNNLLKGIIM GRDGPVPSSR ELIVRPDTLR AIINNRATIE TTTMEAEFTE TLMESNYNS ASVKVSAPFI TANSEYSESS SFKNTETEKS MYTSSRYLFP QGRIDFTTPD SGFDDVIKLS PQFTSGVQAA L AKATGTEK ...String:
HHHHHHHHSQ AGDTLNDVIQ DPTRRNKLIN DNNLLKGIIM GRDGPVPSSR ELIVRPDTLR AIINNRATIE TTTMEAEFTE TLMESNYNS ASVKVSAPFI TANSEYSESS SFKNTETEKS MYTSSRYLFP QGRIDFTTPD SGFDDVIKLS PQFTSGVQAA L AKATGTEK REALQNLFQE YGHVFRTKVH IGGVLSAHTM ETFSRSENET EVKQDVKAGL EGAVKGWGGG ATAGHGNTQG TI TTSQNRK LNVKYIVNGG DYTKIQNTEE WVASTNQSEH WRVIEVTEVT AVADLLPQPI RGQVKDLLKP LLGKWVDVEK VPG LESLPV SVYRPKGAIP AGWFWLGDTA DASKALLVKP TLPARSGRNP ALTSLHQGSG MTEQPFVDLP QYQYLSTYFG SFAH DTPPG STLRGLRPDH VLPGRYEMHG DTISTAVYVT RPVDVPFPED ECFDLKSLVR VKLPGSGNPP KPRSALKKSM VLFDS GEK

UniProtKB: Pleurotolysin B

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Macromolecule #2: Ostreolysin A6

MacromoleculeName: Ostreolysin A6 / type: protein_or_peptide / ID: 2 / Number of copies: 26 / Enantiomer: LEVO
Source (natural)Organism: Pleurotus ostreatus (oyster mushroom)
Molecular weightTheoretical: 15.759398 KDa
Recombinant expressionOrganism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
SequenceString:
MAYAQWVIII IHNVGSQDVK IKNLKASWGK LHADGDKDAE VSASNYEGKI VKPDEKLQIN ASGRSDAAEG TTGTFDLVDP ADGDKQVRH FYWDSPWGSK TNTWTVSGSN TKWMIEYSGQ NLDSGALGTI TVDTLKKGEN LYFQ

UniProtKB: Ostreolysin A6

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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: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 52.0 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: 0.9 µm
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: INSILICO MODEL
Final reconstructionApplied symmetry - Point group: C13 (13 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 2.47 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 73022
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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