ArticleCommunications biology2023
Alternating L4 loop architecture of the bacterial polysaccharide co-polymerase WzzE.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 7 citations in OpenAlex.
- Chain-Length Regulation by WzzE Is Necessary for, but Genetically Separable From, Cyclic Enterobacterial Common Antigen Synthesis.Molecular microbiology · 2026Article
- Structural Basis of Lipopolysaccharide O-Antigen Chain Length Modality.Research (Washington, D.C.) · 2026Article
- Disruption of intestinal barrier and dysbiosis of gut microbiota in an experimental rhesus macaque model with 6-year diabetes mellitus.Experimental animals · 2025Article
- Recent insights into Wzy polymerases and lipopolysaccharide O-antigen biosynthesis.Journal of bacteriology · 2025Review
- Recent advances in understanding of enterobacterial common antigen synthesis and regulation.Open biology · 2025Review
- Genomic characterization and probiotic potential assessment of an exopolysaccharide-producing strain Pediococcus pentosaceus LL-07 isolated from fermented meat.BMC microbiology · 2024Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipopolysaccharides such as the enterobacterial common antigen are important components of the enterobacterial cell envelope that act as a protective barrier against the environment and are often polymerized by the inner membrane bound Wzy-dependent pathway. By employing cryo-electron microscopy we show that WzzE, the co-polymerase component of this pathway that is responsible for the length modulation of the enterobacterial common antigen, is octameric with alternating up-down conformations of its L4 loops. The alternating up-down nature of these essential loops, located at the top of the periplasmic bell, are modulated by clashing helical faces between adjacent protomers that flank the L4 loops around the octameric periplasmic bell. This alternating arrangement and a highly negatively charged binding face create a dynamic environment in which the polysaccharide chain is extended, and suggest a ratchet-type mechanism for polysaccharide elongation.
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Registered trials
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