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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Alkaline Phosphatase / chemistry
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Alkaline Phosphatase / genetics
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Alkaline Phosphatase / metabolism
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Alkaline Phosphatase / ultrastructure
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Amyloid / chemistry*
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Amyloid / genetics
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Amyloid / metabolism
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Amyloid / ultrastructure
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Bacterial Proteins / ultrastructure
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Calcium / chemistry*
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Calcium / metabolism
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Circular Dichroism
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Green Fluorescent Proteins / chemistry
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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Green Fluorescent Proteins / ultrastructure
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Kinetics
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Metalloexopeptidases / chemistry*
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Metalloexopeptidases / genetics
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Metalloexopeptidases / metabolism
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Metalloexopeptidases / ultrastructure
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Microscopy, Electron, Scanning
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Microscopy, Electron, Transmission
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Models, Molecular*
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Polymerization
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Protein Aggregation, Pathological
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Protein Engineering
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Protein Folding
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Protein Interaction Domains and Motifs
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Pseudomonas aeruginosa / enzymology*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Recombinant Fusion Proteins / ultrastructure
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Repetitive Sequences, Amino Acid
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Serine Endopeptidases / chemistry
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Serine Endopeptidases / genetics
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Serine Endopeptidases / metabolism
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Serine Endopeptidases / ultrastructure
Substances
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Amyloid
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Bacterial Proteins
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Recombinant Fusion Proteins
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Green Fluorescent Proteins
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Alkaline Phosphatase
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AprP protease, Pseudomonas
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Metalloexopeptidases
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Pseudomonas serine proteinase
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Serine Endopeptidases
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Calcium