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• W2334152034 endingPage "6462" @default.
• W2334152034 startingPage "6452" @default.
• W2334152034 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." @default.
• W2334152034 created "2016-06-24" @default.
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• W2334152034 date "2014-10-03" @default.
• W2334152034 modified "2023-09-28" @default.
• W2334152034 title "Inducible Polymerization and Two-Dimensional Assembly of the Repeats-in-Toxin (RTX) Domain from the <i>Pseudomonas aeruginosa</i> Alkaline Protease" @default.
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• W2334152034 doi "https://doi.org/10.1021/bi5007546" @default.
• W2334152034 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4204888" @default.
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