1. Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.
- Author
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Zhang L, Franks J, Stolz DB, Conway JF, and Thibodeau PH
- Subjects
- Alkaline Phosphatase chemistry, Alkaline Phosphatase genetics, Alkaline Phosphatase metabolism, Alkaline Phosphatase ultrastructure, Amyloid genetics, Amyloid metabolism, Amyloid ultrastructure, Bacterial Proteins genetics, Bacterial Proteins metabolism, Bacterial Proteins ultrastructure, Calcium metabolism, Circular Dichroism, Green Fluorescent Proteins chemistry, Green Fluorescent Proteins genetics, Green Fluorescent Proteins metabolism, Green Fluorescent Proteins ultrastructure, Kinetics, Metalloexopeptidases genetics, Metalloexopeptidases metabolism, Metalloexopeptidases ultrastructure, Microscopy, Electron, Scanning, Microscopy, Electron, Transmission, Polymerization, Protein Aggregation, Pathological, Protein Engineering, Protein Folding, Protein Interaction Domains and Motifs, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins metabolism, Recombinant Fusion Proteins ultrastructure, Repetitive Sequences, Amino Acid, Serine Endopeptidases chemistry, Serine Endopeptidases genetics, Serine Endopeptidases metabolism, Serine Endopeptidases ultrastructure, Amyloid chemistry, Bacterial Proteins chemistry, Calcium chemistry, Metalloexopeptidases chemistry, Models, Molecular, Pseudomonas aeruginosa enzymology
- Abstract
Self-assembling proteins represent potential scaffolds for the organization of enzymatic activities. The alkaline protease repeats-in-toxin (RTX) domain from Pseudomonas aeruginosa undergoes multiple structural transitions in the presence and absence of calcium, a native structural cofactor. In the absence of calcium, this domain is capable of spontaneous, ordered polymerization, producing amyloid-like fibrils and large two-dimensional protein sheets. This polymerization occurs under near-physiological conditions, is rapid, and can be controlled by regulating calcium in solution. Fusion of the RTX domain to a soluble protein results in the incorporation of engineered protein function into these macromolecular assemblies. Applications of this protein sequence in bacterial adherence and colonization and the generation of biomaterials are discussed.
- Published
- 2014
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