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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Psl polysaccharide related protein structures | |||||||||
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Keywords | complex / PROTEIN TRANSPORT | |||||||||
| Function / homology | Function and homology informationTransferases; 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 | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.89 Å | |||||||||
Authors | Jiao L / Yihua H | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural insights into PSL polysaccharide assembly and export to the cell surface via the Wzx/Wzy-dependent pathway. Authors: Jiao Liu / Yanlong Han / Lanxin Wang / Luyan Z Ma / Dongchun Ni / Yihua Huang / ![]() Abstract: Bacterial extracellular polysaccharides play a crucial role in mediating pathogen-host interactions and bacterial fitness via biofilm formation. The Wzx/Wzy-dependent pathway is the most prevalent ...Bacterial extracellular polysaccharides play a crucial role in mediating pathogen-host interactions and bacterial fitness via biofilm formation. The Wzx/Wzy-dependent pathway is the most prevalent and conserved strategy for polysaccharide biosynthesis. Psl (polysaccharide synthesis locus) is a key biofilm matrix polysaccharide in Pseudomonas aeruginosa PAO1, and its biosynthesis machinery is predicted to be a Wzx/Wzy-dependent biosynthesis system. Here, using Psl in PAO1 as a model strain, we determine the cryo-EM structures of the PslD-PslE complex. These structures reveal that PslD-PslE complex forms a continuous, protected conduit across the entire cell envelope. Further structural and functional analyses demonstrate that the polymerase PslJ, is likely localized in the membrane lumen formed by the octameric arrangement of PslE's transmembrane helical pairs. We propose a mechanistic model in which Und-PP-linked pentasaccharide units of Psl access PslJ through side portals in the PslE octamer, shielding the polymerization and translocation processes from degradation by PlsG, a periplasm-localized endoglycosidase. The iterative addition of incoming repeat units to the reducing terminus of the growing polysaccharide chain is hypothesized to drive Psl export through the channel, a mechanism that may be conserved across the Wzx/Wzy-dependent polysaccharide biosynthesis pathways. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_64810.map.gz | 944.7 MB | EMDB map data format | |
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| Header (meta data) | emd-64810-v30.xml emd-64810.xml | 21.5 KB 21.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_64810_fsc.xml | 21.1 KB | Display | FSC data file |
| Images | emd_64810.png | 79.2 KB | ||
| Filedesc metadata | emd-64810.cif.gz | 6.5 KB | ||
| Others | emd_64810_additional_1.map.gz emd_64810_half_map_1.map.gz emd_64810_half_map_2.map.gz | 719.8 MB 926.5 MB 926.5 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-64810 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-64810 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9v75MC ![]() 9v6lC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_64810.map.gz / Format: CCP4 / Size: 1000 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.03 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_64810_additional_1.map | ||||||||||||
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-Half map: #2
| File | emd_64810_half_map_1.map | ||||||||||||
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-Half map: #1
| File | emd_64810_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : dual complex of Psl transport channel PslD and PslE
| Entire | Name: dual complex of Psl transport channel PslD and PslE |
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| Components |
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-Supramolecule #1: dual complex of Psl transport channel PslD and PslE
| Supramolecule | Name: dual complex of Psl transport channel PslD and PslE / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 828 MDa |
-Macromolecule #1: Biofilm formation protein PslE
| Macromolecule | Name: 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 |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 74.543523 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: 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 |
-Macromolecule #2: Biofilm formation protein PslD
| Macromolecule | Name: Biofilm formation protein PslD / type: protein_or_peptide / ID: 2 / Number of copies: 8 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 27.938232 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: 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 |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 8 |
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| Vitrification | Cryogen name: NITROGEN |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination 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 stage | Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
China, 1 items
Citation







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Processing
FIELD EMISSION GUN

