ArticleThe Journal of biological chemistry2013
Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 59 citations in OpenAlex.
- MucD regulates alginate biosynthesis through the proteolytic control of AlgX and AlgK in Pseudomonas aeruginosa.PLoS biology · 2026Article
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- Applying a polysaccharide lyase fromApplied and environmental microbiology · 2025Article
- Advances in alginate biosynthesis: regulation and production inFrontiers in bioengineering and biotechnology · 2025Review
- Plant Cell Wall PolysaccharidePlants (Basel, Switzerland) · 2024Review
- Pseudomonas aeruginosa biofilm exopolysaccharides: assembly, function, and degradation.FEMS microbiology reviews · 2023Review
- Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa.Nature communications · 2022Article
- The SGNH hydrolase family: a template for carbohydrate diversity.Glycobiology · 2022Review
- Weaving of bacterial cellulose by the Bcs secretion systems.FEMS microbiology reviews · 2022Review
- Comparison of Biochemical Characteristics, Action Models, and Enzymatic Mechanisms of a Novel Exolytic and Two Endolytic Lyases with Mannuronate Preference.Marine drugs · 2021Article
- Structural and mechanistic basis of capsule O-acetylation in Neisseria meningitidis serogroup A.Nature communications · 2020Article
- Structural insights into the putative bacterial acetylcholinesterase ChoE and its substrate inhibition mechanism.The Journal of biological chemistry · 2020Article
- Identification of the Clostridial cellulose synthase and characterization of the cognate glycosyl hydrolase, CcsZ.PloS one · 2020Article
- A Bifunctional UDP-Sugar 4-Epimerase Supports Biosynthesis of Multiple Cell Surface Polysaccharides in Sinorhizobium meliloti.Journal of bacteriology · 2019Article
- A partial reconstitution implicates DltD in catalyzing lipoteichoic acid d-alanylation.The Journal of biological chemistry · 2018Article
- Article
- Mechanistic Pathways for Peptidoglycan O-Acetylation and De-O-Acetylation.Frontiers in microbiology · 2018Review
- PatB1 is an O-acetyltransferase that decorates secondary cell wall polysaccharides.Nature chemical biology · 2018Article
- Biological function of a polysaccharide degrading enzyme in the periplasm.Scientific reports · 2016Article
- Analysis of respiratory activity and carbon usage of a mutant of Azotobacter vinelandii impaired in poly-β-hydroxybutyrate synthesis.Journal of industrial microbiology & biotechnology · 2016Article
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
Abstract
The exopolysaccharide alginate, produced by mucoid Pseudomonas aeruginosa in the lungs of cystic fibrosis patients, undergoes two different chemical modifications as it is synthesized that alter the properties of the polymer and hence the biofilm. One modification, acetylation, causes the cells in the biofilm to adhere better to lung epithelium, form microcolonies, and resist the effects of the host immune system and/or antibiotics. Alginate biosynthesis requires 12 proteins encoded by the algD operon, including AlgX, and although this protein is essential for polymer production, its exact role is unknown. In this study, we present the X-ray crystal structure of AlgX at 2.15 Å resolution. The structure reveals that AlgX is a two-domain protein, with an N-terminal domain with structural homology to members of the SGNH hydrolase superfamily and a C-terminal carbohydrate-binding module. A number of residues in the carbohydrate-binding module form a substrate recognition "pinch point" that we propose aids in alginate binding and orientation. Although the topology of the N-terminal domain deviates from canonical SGNH hydrolases, the residues that constitute the Ser-His-Asp catalytic triad characteristic of this family are structurally conserved. In vivo studies reveal that site-specific mutation of these residues results in non-acetylated alginate. This catalytic triad is also required for acetylesterase activity in vitro. Our data suggest that not only does AlgX protect the polymer as it passages through the periplasm but that it also plays a role in alginate acetylation. Our results provide the first structural insight for a wide group of closely related bacterial polysaccharide acetyltransferases.
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