Abstract 2424 Defining structure and function of GT-A fold enzymes in bacterial glycan assembly
Bacterial glycoconjugates mediate vital bacterial pathogen– host interactions and are also essential for bacterial survival. The machinery involved in bacterial glycoconjugate biosynthesis comprises an emerging set of antibiotic targets. The glycosyltransferase PglI attaches a branching glycan to the undecaprenyl phosphate-linked glycopolymer substrate. The branching position of the sugar varies widely amongst the different species of Campylobacter and the mode of action and structural determinants of PglI specificity are not known.
Authors
- Barbara Imperiali (ORCID: https://orcid.org/0000-0002-5749-7869)
- Karen N. Allen (ORCID: https://orcid.org/0000-0001-7296-0551)
- Christine A. Arbour (ORCID: https://orcid.org/0000-0001-6056-296X)
- Hayley Knox (ORCID: https://orcid.org/0000-0003-1467-309X)
Institutions
- Boston University (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109339
- Primary Topic
- Enzyme Production and Characterization
- Type
- article
- Field-Weighted Citation Impact
- 0.00