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- EMDB-64810: Psl polysaccharide related protein structures -

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Basic information

Entry
Database: EMDB / ID: EMD-64810
TitlePsl polysaccharide related protein structures
Map data
Sample
  • Complex: dual complex of Psl transport channel PslD and PslE
    • Protein or peptide: Biofilm formation protein PslE
    • Protein or peptide: Biofilm formation protein PslD
Keywordscomplex / PROTEIN TRANSPORT
Function / homology
Function and homology information


Transferases; Transferring phosphorus-containing groups; Protein-tyrosine kinases / polysaccharide transmembrane transporter activity / porin activity / pore complex / monoatomic ion transport / cell outer membrane / protein tyrosine kinase activity / plasma membrane
Similarity search - Function
Polysaccharide export protein / : / Polysaccharide biosynthesis/export protein / : / : / SLBB domain / Prokaryotic membrane lipoprotein lipid attachment site profile. / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biofilm formation protein PslE / Biofilm formation protein PslD
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.89 Å
AuthorsJiao L / Yihua H
Funding support China, 1 items
OrganizationGrant numberCountry
Chinese Academy of Sciences China
CitationJournal: To Be Published
Title: Psl polysaccharide related protein structures
Authors: Jiao L / Jiao L
History
DepositionMay 27, 2025-
Header (metadata) releaseJun 3, 2026-
Map releaseJun 3, 2026-
UpdateJun 3, 2026-
Current statusJun 3, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

Downloads & links

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Map

FileDownload / File: emd_64810.map.gz / Format: CCP4 / Size: 1000 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.03 Å/pix.
x 640 pix.
= 659.2 Å
1.03 Å/pix.
x 640 pix.
= 659.2 Å
1.03 Å/pix.
x 640 pix.
= 659.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.03 Å
Density
Contour LevelBy AUTHOR: 0.803
Minimum - Maximum-1.9399434 - 4.483198
Average (Standard dev.)-0.0004879072 (±0.093900315)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions640640640
Spacing640640640
CellA=B=C: 659.19995 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_64810_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #2

Fileemd_64810_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Half map: #1

Fileemd_64810_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : dual complex of Psl transport channel PslD and PslE

EntireName: dual complex of Psl transport channel PslD and PslE
Components
  • Complex: dual complex of Psl transport channel PslD and PslE
    • Protein or peptide: Biofilm formation protein PslE
    • Protein or peptide: Biofilm formation protein PslD

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Supramolecule #1: dual complex of Psl transport channel PslD and PslE

SupramoleculeName: dual complex of Psl transport channel PslD and PslE / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 828 MDa

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Macromolecule #1: Biofilm formation protein PslE

MacromoleculeName: Biofilm formation protein PslE / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO
EC number: Transferases; Transferring phosphorus-containing groups; Protein-tyrosine kinases
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 74.543523 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MIEIRSLRDL LRLLFIYQRE FKLAALSAVV IIVLGAFLLP AKYESNARLL VKPGRDSTLP IEISNRQALV MPSTQRDPIV DEERLLTGR PIVRQVAERY LEVLANRPPP EGLWKRTKFY VKKAIGAVFD GIRVTLETFG VIEETTAVER LAKDLEKKFE V THAAGSTV ...String:
MIEIRSLRDL LRLLFIYQRE FKLAALSAVV IIVLGAFLLP AKYESNARLL VKPGRDSTLP IEISNRQALV MPSTQRDPIV DEERLLTGR PIVRQVAERY LEVLANRPPP EGLWKRTKFY VKKAIGAVFD GIRVTLETFG VIEETTAVER LAKDLEKKFE V THAAGSTV MEISFTWSEP EVAQEVVKAW IEIYMEERTQ ALGRKSLYAF YEAQTADSAA QIKSYKAQIL KHLNEIGASS IE DRLQDLS ERINVLRGER FNSIRLIASS DSALESTRQQ LKGLPREIVT VRQIALNPAQ QDLRRLLNQK RLERADMMRT YTD DAPPVK ALDASIRALE KEVQDEGATV QSSEDRAPNT LTTHLERVLL DETSNNAALR TQLAEQEKQL AELEAQRREA LDIE PTLAR LQRELNATER NYALYVDSLE KSRIDRELDK SQISNISVIE EATYNPGRIF PKTLLMLFLA VPFGLAVGLL VVYLC YLLD QRIHDGGLVE EKFGLPLWTT LPELSNSTAE SSNAFTASIC RLYGLLPYAR IEEKGLTLGL TSARHGEGVT FIIEQL RRL LEENGVRVRI GGEPAQPGEV VLLDAPALLD SCEAFIALRR ADLIALVVEA QKSTVPVVEH ALTILTTAFG KVDGIII NR RRFEVPSKVL QTIARYRSAF

UniProtKB: Biofilm formation protein PslE

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Macromolecule #2: Biofilm formation protein PslD

MacromoleculeName: Biofilm formation protein PslD / type: protein_or_peptide / ID: 2 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Pseudomonas aeruginosa (bacteria)
Molecular weightTheoretical: 27.938232 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKRTLLMLAM LALAACNTPA RIPAPDSDTV DSGKRALEEL ARLPPAMERV RVGDTLRIVR DAGEMPTLSA FNVATIYELT LYTVLNDGS IYYPFIGRIQ AAHRTPQEIA NELTTKLAPI YREPRVTVNI NQAPGNTVFV GGAVRNPSAV PIPAANNMEQ A ILGAGGIL ...String:
MKRTLLMLAM LALAACNTPA RIPAPDSDTV DSGKRALEEL ARLPPAMERV RVGDTLRIVR DAGEMPTLSA FNVATIYELT LYTVLNDGS IYYPFIGRIQ AAHRTPQEIA NELTTKLAPI YREPRVTVNI NQAPGNTVFV GGAVRNPSAV PIPAANNMEQ A ILGAGGIL PVGDARRVAL MREDSEGRYH AYFLDFSQLM KIGPEGRKPL AMQRGDIVFV PKSMVGDRIE GVDVYLNQLL PF AKSIGVG VSYTVNNDR

UniProtKB: Biofilm formation protein PslD

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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: NITROGEN

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 96000
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: NONE
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.89 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 116722
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

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