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Microbiology
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- ArticleOpen Access
Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen from Escherichia coli O9a
Journal of Biological ChemistryVol. 294Issue 41p14978–14990Published online: August 15, 2019- Evan Mann
- Steven D. Kelly
- M. Sameer Al-Abdul-Wahid
- Bradley R. Clarke
- Olga G. Ovchinnikova
- Bin Liu
- and others
Cited in Scopus: 8Escherichia coli serotype O9a provides a model for export of lipopolysaccharide (LPS) O-antigen polysaccharide (O-PS) via ABC transporters. In O9a biosynthesis, a chain-terminator enzyme, WbdD, caps the nonreducing end of the glycan with a methylphosphate moiety and thereby establishes chain-length distribution. A carbohydrate-binding module (CBM) in the ABC transporter recognizes terminated glycans, ensuring that only mature O-PS is exported and incorporated into LPS. Here, we addressed two questions arising from this model.