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| Title | Structural Basis of Lipopolysaccharide O-Antigen Chain Length Modality. |
|---|---|
| Journal, issue, pages | Research (Wash D C), Vol. 9, Page 1276, Year 2026 |
| Publish date | May 12, 2026 |
Authors | Benjamin Wiseman / Göran Widmalm / Martin Högbom / ![]() |
| PubMed Abstract | Lipopolysaccharides are important components of the gram-negative bacterial cell envelope that are involved in immune evasion and act as a protective barrier. Employing cryo-electron microscopy, we ...Lipopolysaccharides are important components of the gram-negative bacterial cell envelope that are involved in immune evasion and act as a protective barrier. Employing cryo-electron microscopy, we resolved the structure and dynamics of FepE, the copolymerase component of the Wzy-dependent pathway, responsible for the length modulation of very long O-antigen molecules. Comparison of the interior volumes of related copolymerases' periplasmic domains with the volume of hydrated sugars suggests that the size of the periplasmic domain controls the length of the O-antigen, implying that polysaccharide chain polymerization occurs inside the copolymerase periplasmic domain. Moreover, we show the opening of the FepE complex as well as other large mechanistically relevant movements. The opening of the complex presents an attractive corridor for the release of completed polysaccharide chains. |
External links | Research (Wash D C) / PubMed:42131584 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.8 - 3.4 Å |
| Structure data | EMDB-54965, PDB-9ski: EMDB-54966, PDB-9skj: EMDB-54967, PDB-9skk: EMDB-54968, PDB-9skl: ![]() EMDB-54969: Polysaccharide co-polymerase closed FepE 9 subunit complex C1 symmetry. |
| Source |
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Keywords | MEMBRANE PROTEIN / enzyme / polysaccharide / co-polymerase |
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