Inducible Polymerization and Two-Dimensional Assembly of the Repeats-in-Toxin (RTX) Domain from thePseudomonas aeruginosaAlkaline Protease | Zendy

Liang Zhang | Zendy; Jonathon Franks | Zendy; Donna B. Stolz | Zendy; James F. Conway | Zendy; Patrick H. Thibodeau | Zendy

Open Access

Inducible Polymerization and Two-Dimensional Assembly of the Repeats-in-Toxin (RTX) Domain from thePseudomonas aeruginosaAlkaline Protease

Author(s) -

Liang Zhang,

Jonathon Franks,

Donna B. Stolz,

James F. Conway,

Patrick H. Thibodeau

Publication year - 2014

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi5007546

Subject(s) - protease , chemistry , polymerization , fusion protein , calcium , pseudomonas aeruginosa , protein domain , biophysics , biochemistry , enzyme , recombinant dna , microbiology and biotechnology , biology , bacteria , polymer , genetics , gene , organic chemistry

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.

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