Summary for 9R66
| Entry DOI | 10.2210/pdb9r66/pdb |
| EMDB information | 53604 |
| Descriptor | Putative polysaccharide export protein Wza, Tyrosine-protein kinase wzc, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | cps transporter, transport protein |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 16 |
| Total formula weight | 1006864.95 |
| Authors | Yuan, B.,Heinz, D.W. (deposition date: 2025-05-11, release date: 2026-03-04, Last modification date: 2026-07-29) |
| Primary citation | Yuan, B.,Sieben, C.,Raj, P.,Rietschel, T.,Hennell James, R.,Gatzemeier, A.,Jansch, L.,Marlovits, T.C.,Heinz, D.W. Molecular insights into the capsular polysaccharide transporter Wza-Wzc complex. Nat Commun, 17:1436-1436, 2026 Cited by PubMed 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 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. PubMed: 41644548DOI: 10.1038/s41467-026-69136-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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