26GS
Colanic acid polysaccharide related protein structures
Summary for 26GS
| Entry DOI | 10.2210/pdb26gs/pdb |
| EMDB information | 80645 |
| Descriptor | Tyrosine-protein kinase wzc, Putative polysaccharide export protein Wza (2 entities in total) |
| Functional Keywords | complex, protein transport |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 16 |
| Total formula weight | 659209.40 |
| Authors | jiao, L.,Yanlong, H. (deposition date: 2026-04-29, release date: 2026-06-24, Last modification date: 2026-07-22) |
| Primary citation | Liu, J.,Han, Y.,Huang, G.,Zhang, M.,Du, J.,Zhou, H.,Chen, D.,Huang, Y. Architecture of the Wza-Wzc complex that mediates colanic acid translocation across the cell envelope in Gram-negative bacteria. Nat Commun, 2026 Cited by PubMed Abstract: The Wzx/Wzy-dependent pathway is a highly conserved mechanism for bacterial polysaccharide biosynthesis. This pathway is exemplified by the assembly and export of colanic acid mediated by the Wza-Wzc complex. While recent structural investigations have yielded valuable insights into the molecular basis of colanic acid biosynthesis, the overall architecture of the Wza-Wzc complex and the regulatory mechanism of colanic acid export remain incompletely understood. Here, we report cryo-electron microscopy (cryo-EM) structures of the Wza-Wzc complex from E. coli K12 in two functionally states: the autophosphorylated wild-type (Wza-Wzc) state and the non-phosphorylated (Wza-Wzc) state. Both structures reveal that Wza and Wzc assemble into a continuous channel spanning the entire bacterial cell envelope, indicating that phosphorylation of Wzc does not disassemble the intact export channel. Relative to Wza-Wzc, the octameric periplasmic domain of Wzc in Wza-Wzc undergoes a significant conformational rearrangement. This rearrangement reduces constriction region's diameter and confers a negatively charged property to the interior of the Wzc octamer, which is proposed to inhibit colanic acid export. Collectively, these structural findings confirm that the Wza-Wzc complex forms a colanic acid export channel throughout Wzc's phosphorylation-dephosphorylation cycle, advancing our mechanistic understanding of the Wzx/Wzy-dependent polysaccharide biosynthesis pathway in Gram-negative bacteria. PubMed: 42399268DOI: 10.1038/s41467-026-75198-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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