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.

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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
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article

Abstract 2424 Defining structure and function of GT-A fold enzymes in bacterial glycan assembly

Barbara Imperiali, Karen N. Allen, Christine A. Arbour, Hayley Knox
1 links
Journal of Biological Chemistry
Enzyme Production and Characterization
article

Abstract 2424 Defining structure and function of GT-A fold enzymes in bacterial glycan assembly

Barbara Imperiali, Karen N. Allen, Christine A. Arbour, Hayley Knox
article en

Abstract

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.

Journal of Biological ChemistryVol. 301(5)
Boston University (US)
Zero hunger
Openalex Percentile: Top 85%
Enzyme Production and Characterization
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