Structural insights into the polytopic Escherichia coli phosphoglycosyl transferase WbaP

Host-pathogen interactions frequently depend on key components of the bacterial cell surface, such as capsules and lipopolysaccharides in Gram-negative bacteria. The first step in the synthesis of lipid-linked polysaccharides is the substitution of a uridine diphosphate (UDP)-sugar by a lipid monophosphate catalysed by a phosphoglycosyl transferase (PGT). We report the 3.0 Å cryo-electron microscopy apo-structure of the PGT enzyme WbaP from Escherichia coli, a UDP-galactose:undecaprenolphosphate galactose-1-phosphoryl transferase. The structure is a dimer with each monomer formed of four N-terminal transmembrane helices, a small α/β domain with a distinctive β-hairpin that inserts into the other monomer, and a catalytic domain, which sits perpendicular to the transmembrane domain. A complex of WbaP with the UDP-galactose substrate shows binding of the UDP moiety by R319 and R377. Mutations of R319 and R377, along with K331 and R401, highlighted the essential nature of these residues for the catalytic activity of the protein, as confirmed by an in vivo functional assay. Our results provide new insights into the PGT family of enzymes.

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Publication Details

Journal
Open Biology
Published
2026-08-19
DOI
https://doi.org/10.1098/rsob.250369
Primary Topic
Carbohydrate Chemistry and Synthesis
Type
article
Field-Weighted Citation Impact
0.00

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article

Structural insights into the polytopic Escherichia coli phosphoglycosyl transferase WbaP

Jan Steyaert, Els Pardon, Peter J. Harrison, Miriam Weckener et al.
Open Biology
Carbohydrate Chemistry and Synthesis
article

Structural insights into the polytopic Escherichia coli phosphoglycosyl transferase WbaP

Jan Steyaert, Els Pardon, Peter J. Harrison, Miriam Weckener, Andrew M. Giltrap, Abirami Lakshminarayanan, Benjamin G. Davis, S.A. McMahon, Huanting Liu, Chris Whitfield, Alice Eddershaw, James H. Naismith, Audrey Le Bas, Philip N. Ward, Bradley R. Clarke
article en

Abstract

Host-pathogen interactions frequently depend on key components of the bacterial cell surface, such as capsules and lipopolysaccharides in Gram-negative bacteria. The first step in the synthesis of lipid-linked polysaccharides is the substitution of a uridine diphosphate (UDP)-sugar by a lipid monophosphate catalysed by a phosphoglycosyl transferase (PGT). We report the 3.0 Å cryo-electron microscopy apo-structure of the PGT enzyme WbaP from Escherichia coli, a UDP-galactose:undecaprenolphosphate galactose-1-phosphoryl transferase. The structure is a dimer with each monomer formed of four N-terminal transmembrane helices, a small α/β domain with a distinctive β-hairpin that inserts into the other monomer, and a catalytic domain, which sits perpendicular to the transmembrane domain. A complex of WbaP with the UDP-galactose substrate shows binding of the UDP moiety by R319 and R377. Mutations of R319 and R377, along with K331 and R401, highlighted the essential nature of these residues for the catalytic activity of the protein, as confirmed by an in vivo functional assay. Our results provide new insights into the PGT family of enzymes.

Open BiologyVol. 16(8)
University of St Andrews (GB), Didcot Community Hospital (GB), Rosalind Franklin Institute (GB), Oxford Applied Research (United Kingdom) (GB), 3E (Belgium) (BE), Science Oxford (GB), University of Guelph (CA)
Rosalind Franklin Institute, Wellcome Trust, UK Research and Innovation, Canadian Institutes of Health Research, Engineering and Physical Sciences Research Council
Openalex Percentile: Top 19%
Carbohydrate Chemistry and Synthesis
DOIOpen Access PDFOpenAlex
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