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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | CPS co-polymerase Wzc_C4 | |||||||||
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Keywords | Capsular polysaccharide secretion pathway / TRANSPORT PROTEIN | |||||||||
| Function / homology | Function and homology informationTransferases; Transferring phosphorus-containing groups; Protein-tyrosine kinases / colanic acid biosynthetic process / polysaccharide biosynthetic process / peptidyl-tyrosine autophosphorylation / protein tyrosine kinase activity / ATP hydrolysis activity / ATP binding / identical protein binding / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Yuan B / Heinz DW | |||||||||
| Funding support | Germany, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: Molecular insights into the capsular polysaccharide transporter Wza-Wzc complex. Authors: Biao Yuan / Christian Sieben / Prateek Raj / Tina Rietschel / Rory Hennell James / Anja Gatzemeier / Lothar Jänsch / Thomas C Marlovits / Dirk W Heinz / ![]() Abstract: Capsular polysaccharides (CPS) are key virulence determinants, constituting the protective capsule that surrounds bacterial pathogens. Here, we present the complete cryo-EM structure of Gram-negative ...Capsular polysaccharides (CPS) are key virulence determinants, constituting the protective capsule that surrounds bacterial pathogens. Here, we present the complete cryo-EM structure of Gram-negative bacterial CPS secretion machinery formed by the E. coli K12 Wza-Wzc complex. The structure reveals an elongated, continuous channel spanning the entire envelope that facilitates CPS secretion. Multiple structural snapshots of the ADP-bound Wza-Wzc complex capture intermediate conformations of the double membrane assembly, highlighting its remarkable intrinsic dynamics. In-depth analysis of the isolated Wza translocon and Wzc co-polymerase, reveals mechanistic details of both complex formation and CPS transport. We further uncover the jellyroll domain of Wzc as a CPS-binding module, likely guiding CPS repeat units into a proposed Wzc-Wzy polymerization platform. Collectively, this work provides structural and functional insights into CPS synthesis and transport, advancing our understanding of bacterial capsule formation and virulence mechanisms. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_53601.map.gz | 168 MB | EMDB map data format | |
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| Header (meta data) | emd-53601-v30.xml emd-53601.xml | 18.7 KB 18.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_53601_fsc.xml | 11.9 KB | Display | FSC data file |
| Images | emd_53601.png | 55.6 KB | ||
| Filedesc metadata | emd-53601.cif.gz | 6.2 KB | ||
| Others | emd_53601_half_map_1.map.gz emd_53601_half_map_2.map.gz | 164.8 MB 164.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-53601 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-53601 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9r63MC ![]() 9r60C ![]() 9r61C ![]() 9r62C ![]() 9r64C ![]() 9r65C ![]() 9r66C ![]() 9r67C ![]() 9r68C ![]() 9r69C ![]() 9r6aC ![]() 9r6bC ![]() 9r6cC 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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Map
| File | Download / File: emd_53601.map.gz / Format: CCP4 / Size: 178 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: 0.91 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_53601_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_53601_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : WzcK540M octamer
| Entire | Name: WzcK540M octamer |
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| Components |
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-Supramolecule #1: WzcK540M octamer
| Supramolecule | Name: WzcK540M octamer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: Tyrosine-protein kinase wzc
| Macromolecule | Name: Tyrosine-protein kinase wzc / 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: 81.557086 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MTEKVKQHAA PVTGSDEIDI GRLVGTVIEA RWWVIGITTV FALCAVVYTF FATPIYSADA LVQIEQNSGN SLVQDIGSAL ANKPPASDA EIQLIRSRLV LGKTVDDLDL DIAVSKNTFP IFGAGWDRLM GRQNETVKVT TFNRPKEMAD QVFTLNVLDN K NYTLSSDG ...String: MTEKVKQHAA PVTGSDEIDI GRLVGTVIEA RWWVIGITTV FALCAVVYTF FATPIYSADA LVQIEQNSGN SLVQDIGSAL ANKPPASDA EIQLIRSRLV LGKTVDDLDL DIAVSKNTFP IFGAGWDRLM GRQNETVKVT TFNRPKEMAD QVFTLNVLDN K NYTLSSDG GFSARGQAGQ MLKKEGVTLM VEAIHASPGS EFTVTKYSTL GMINQLQNSL TVTENGKDAG VLSLTYTGED RE QIRDILN SIARNYQEQN IERKSAEASK SLAFLAQQLP EVRSRLDVAE NKLNAFRQDK DSVDLPLEAK AVLDSMVNID AQL NELTFK EAEISKLYTK VHPAYRTLLE KRQALEDEKA KLNGRVTAMP KTQQEIVRLT RDVESGQQVY MQLLNKEQEL KITE ASTVG DVRIVDPAIT QPGVLKPKKG LIILGAIILG LMLSIVGVLL RSLFNRGIES PQVLEEHGIS VYASIPLSEW QKARD SVKT IKGIKRYKQS QLLAVGNPTD LAIEAIRSLR TSLHFAMMQA QNNVLMMTGV SPSIGMTFVC ANLAAVISQT NKRVLL IDC DMRKGYTHEL LGTNNVNGLS EILIGQGDIT TAAKPTSIAK FDLIPRGQVP PNPSELLMSE RFAELVNWAS KNYDLVL ID TPPILAVTDA AIVGRHVGTT LMVARYAVNT LKEVETSLSR FEQNGIPVKG VILNSIFRRA SAYQDYGYYE YEYKSDAK S SGENLYFQGW SHPQFEK UniProtKB: Tyrosine-protein kinase wzc |
-Macromolecule #2: ADENOSINE-5'-DIPHOSPHATE
| Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 8 / Formula: ADP |
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| Molecular weight | Theoretical: 427.201 Da |
| Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #3: MAGNESIUM ION
| Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 3 / Number of copies: 8 / Formula: MG |
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| Molecular weight | Theoretical: 24.305 Da |
-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: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: DARK FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
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Keywords
Authors
Germany, 1 items
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Processing
FIELD EMISSION GUN
