ArticleActa crystallographica. Section D, Biological crystallography2014
A conformational landscape for alginate secretion across the outer membrane of Pseudomonas aeruginosa.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 51 citations in OpenAlex.
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- 7.10 MAG. A Novel Host Monoacylglyceride forCrystal growth & design · 2024Article
- Pseudomonas aeruginosa biofilm exopolysaccharides: assembly, function, and degradation.FEMS microbiology reviews · 2023Review
- Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.Communications chemistry · 2023Article
- Design of the elusive proteinaceous oxygen donor copper site suggests a promising future for copper for MRI contrast agents.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure-Thermodynamic Relationship of a Polysaccharide Gel (Alginate) as a Function of Water Content and Counterion Type (Na vs Ca).The journal of physical chemistry. B · 2023Article
- Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa.Nature communications · 2022Article
- Bacterial Outer Membrane Polysaccharide Export (OPX) Proteins Occupy Three Structural Classes with Selective β-Barrel Porin Requirements for Polymer Secretion.Microbiology spectrum · 2022Article
- Interactions with Microbial Proteins Driving the Antibacterial Activity of Flavonoids.Pharmaceutics · 2021Review
- Article
- TheThe Journal of biological chemistry · 2020Article
- Architecture of the Cellulose Synthase Outer Membrane Channel and Its Association with the Periplasmic TPR Domain.Structure (London, England : 1993) · 2019Article
- Structural features underlying recognition and translocation of extracellular polysaccharides.Interface focus · 2019Review
- Bacterial Surface Spreading Is More Efficient on Nematically Aligned Polysaccharide Substrates.Journal of bacteriology · 2018Article
- The cubicon method for concentrating membrane proteins in the cubic mesophase.Nature protocols · 2017Article
- A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.Nature communications · 2017Article
- Polymertropism of rod-shaped bacteria: movement along aligned polysaccharide fibers.Scientific reports · 2017Article
- Biological function of a polysaccharide degrading enzyme in the periplasm.Scientific reports · 2016Article
- Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane.The Journal of biological chemistry · 2016Article
- Alginate Biosynthesis Factories in Pseudomonas fluorescens: Localization and Correlation with Alginate Production Level.Applied and environmental microbiology · 2016Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
The exopolysaccharide alginate is an important component of biofilms produced by Pseudomonas aeruginosa, a major pathogen that contributes to the demise of cystic fibrosis patients. Alginate exits the cell via the outer membrane porin AlgE. X-ray structures of several AlgE crystal forms are reported here. Whilst all share a common β-barrel constitution, they differ in the degree to which loops L2 and T8 are ordered. L2 and T8 have been identified as an extracellular gate (E-gate) and a periplasmic gate (P-gate), respectively, that reside on either side of an alginate-selectivity pore located midway through AlgE. Passage of alginate across the membrane is proposed to be regulated by the sequential opening and closing of the two gates. In one crystal form, the selectivity pore contains a bound citrate. Because citrate mimics the uronate monomers of alginate, its location is taken to highlight a route through AlgE taken by alginate as it crosses the pore. Docking and molecular-dynamics simulations support and extend the proposed transport mechanism. Specifically, the P-gate and E-gate are flexible and move between open and closed states. Citrate can leave the selectivity pore bidirectionally. Alginate docks stably in a linear conformation through the open pore. To translate across the pore, a force is required that presumably is provided by the alginate-synthesis machinery. Accessing the open pore is facilitated by complex formation between AlgE and the periplasmic protein AlgK. Alginate can thread through a continuous pore in the complex, suggesting that AlgK pre-orients newly synthesized exopolysaccharide for delivery to AlgE.
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