ArticleThe Journal of biological chemistry2012
The structure- and metal-dependent activity of Escherichia coli PgaB provides insight into the partial de-N-acetylation of poly-β-1,6-N-acetyl-D-glucosamine.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 78 citations in OpenAlex.
- Biochemical and Structural Characterization of Two-domain Glycoside Hydrolase PgaB fromACS infectious diseases · 2026Article
- Biofilm-mediated antibiotic cross-protection:Microbiology spectrum · 2026Article
- Bacillus cereus PelAThe Journal of biological chemistry · 2026Article
- Matrine Restores Porcine-Origin β-Lactam-ResistantAntibiotics (Basel, Switzerland) · 2026Article
- Structural and functional analysis of Pseudomonas aeruginosa PelA provides insight into the modification of the Pel exopolysaccharide.The Journal of biological chemistry · 2025Article
- Expansion of the diversity of dispersin scaffolds.Acta crystallographica. Section D, Structural biology · 2025Article
- Carbohydrate Deacetylase Unique to Gut Microbe Bacteroides Reveals Atypical Structure.Biochemistry · 2025Article
- The deficiency of poly-β-1,6-N-acetyl-glucosamine deacetylase trigger A. baumannii to convert to biofilm-independent colistin-tolerant cells.Scientific reports · 2023Article
- Functional analysis of the N-terminal region of acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis.FEBS open bio · 2022Article
- The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing.PLoS pathogens · 2022Article
- Identification of Potential Insect Growth Inhibitor againstInternational journal of molecular sciences · 2022Article
- PplD is a de-N-acetylase of the cell wall linkage unit of streptococcal rhamnopolysaccharides.Nature communications · 2022Article
- Article
- Mitigating Milk-Associated Bacteria through Inducing Zinc Ions Antibiofilm Activity.Foods (Basel, Switzerland) · 2020Article
- Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation.Nature communications · 2020Article
- A systematic pipeline for classifying bacterial operons reveals the evolutionary landscape of biofilm machineries.PLoS computational biology · 2020Article
- Structural and biochemical insights into the catalytic mechanisms of two insect chitin deacetylases of the carbohydrate esterase 4 family.The Journal of biological chemistry · 2019Article
- PgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-β(1,6)-N-acetylglucosamine and can disrupt bacterial biofilms.PLoS pathogens · 2018Article
- Substrate Recognition and Specificity of Chitin Deacetylases and Related Family 4 Carbohydrate Esterases.International journal of molecular sciences · 2018Review
- Structural and chemical biology of deacetylases for carbohydrates, proteins, small molecules and histones.Communications biology · 2018Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Exopolysaccharides are required for the development and integrity of biofilms produced by a wide variety of bacteria. In Escherichia coli, partial de-N-acetylation of the exopolysaccharide poly-β-1,6-N-acetyl-D-glucosamine (PNAG) by the periplasmic protein PgaB is required for polysaccharide intercellular adhesin-dependent biofilm formation. To understand the molecular basis for PNAG de-N-acetylation, the structure of PgaB in complex with Ni(2+) and Fe(3+) have been determined to 1.9 and 2.1 Å resolution, respectively, and its activity on β-1,6-GlcNAc oligomers has been characterized. The structure of PgaB reveals two (β/α)(x) barrel domains: a metal-binding de-N-acetylase that is a member of the family 4 carbohydrate esterases (CE4s) and a domain structurally similar to glycoside hydrolases. PgaB displays de-N-acetylase activity on β-1,6-GlcNAc oligomers but not on the β-1,4-(GlcNAc)(4) oligomer chitotetraose and is the first CE4 member to exhibit this substrate specificity. De-N-acetylation occurs in a length-dependent manor, and specificity is observed for the position of de-N-acetylation. A key aspartic acid involved in de-N-acetylation, normally seen in other CE4s, is missing in PgaB, suggesting that the activity of PgaB is attenuated to maintain the low levels of de-N-acetylation of PNAG observed in vivo. The metal dependence of PgaB is different from most CE4s, because PgaB shows increased rates of de-N-acetylation with Co(2+) and Ni(2+) under aerobic conditions, and Co(2+), Ni(2+) and Fe(2+) under anaerobic conditions, but decreased activity with Zn(2+). The work presented herein will guide inhibitor design to combat biofilm formation by E. coli and potentially a wide range of medically relevant bacteria producing polysaccharide intercellular adhesin-dependent biofilms.
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