ArticleJournal of bacteriology2007
Functional characterization and membrane topology of Escherichia coli WecA, a sugar-phosphate transferase initiating the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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70 citing papers in PubMed.
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- Differential substrate preferences IN ACTINOBACTERIAL protein O-MANNOSYLTRANSFERASES and alteration of protein-O-MANNOSYLATION by choice of secretion pathway.Glycobiology · 2025Article
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- Uridine Bisphosphonates Differentiate Phosphoglycosyl Transferase Superfamilies.Journal of the American Chemical Society · 2024Article
- Natural reversion promotes LPS elongation in an attenuated Coxiella burnetii strain.Nature communications · 2024Article
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- Structural and Genetic Identification of the O-Antigen from anInternational journal of molecular sciences · 2023Article
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- Characterization and the host specificity of Pet-CM3-4, a new phage infecting Cronobacter and Enterobacter strains.Virus research · 2023Article
- A New Face of the Old Gene: Deletion of theInternational journal of molecular sciences · 2023Article
- The evolution of antibiotic resistance in an incurable and ultimately fatal infection: A retrospective case study.Evolution, medicine, and public health · 2023Article
- A bioconjugate vaccine againstFrontiers in bioengineering and biotechnology · 2023Article
- Probing Monotopic Phosphoglycosyl Transferases from Complex Cellular Milieu.ACS chemical biology · 2022Article
- Modification of avian pathogenic Escherichia coli χ7122 lipopolysaccharide increases accessibility to glycoconjugate antigens.Microbial cell factories · 2022Article
10 more citing papers are in PubMed but not listed here.
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
WecA is an integral membrane protein that initiates the biosynthesis of enterobacterial common antigen and O-antigen lipopolysaccharide (LPS) by catalyzing the transfer of N-acetylglucosamine (GlcNAc)-1-phosphate onto undecaprenyl phosphate (Und-P) to form Und-P-P-GlcNAc. WecA belongs to a large family of eukaryotic and prokaryotic prenyl sugar transferases. Conserved aspartic acids in putative cytoplasmic loops 2 (Asp90 and Asp91) and 3 (Asp156 and Asp159) were targeted for replacement mutagenesis with either glutamic acid or asparagine. We examined the ability of each mutant protein to complement O-antigen LPS synthesis in a wecA-deficient strain and also determined the steady-state kinetic parameters of the mutant proteins in an in vitro transfer assay. Apparent K(m) and V(max) values for UDP-GlcNAc, Mg(2+), and Mn(2+) suggest that Asp156 is required for catalysis, while Asp91 appears to interact preferentially with Mg(2+), possibly playing a role in orienting the substrates. Topological analysis using the substituted cysteine accessibility method demonstrated the cytosolic location of Asp90, Asp91, and Asp156 and provided a more refined overall topological map of WecA. Also, we show that cells expressing a WecA derivative C terminally fused with the green fluorescent protein exhibited a punctate distribution of fluorescence on the bacterial surface, suggesting that WecA localizes to discrete regions in the bacterial plasma membrane.
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