title: Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.
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.
authors.affiliation: Departments of Cell Biology and ‡Structural Biology, The University of Pittsburgh School of Medicine , Pittsburgh, Pennsylvania 15261, United States.
authors.forename: Liang
authors.initials: L
authors.lastname: Zhang
authors.forename: Jonathon
authors.initials: J
authors.lastname: Franks
authors.forename: Donna B
authors.initials: DB
authors.lastname: Stolz
authors.forename: James F
authors.initials: JF
authors.lastname: Conway
authors.forename: Patrick H
authors.initials: PH
authors.lastname: Thibodeau
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D000682:Amyloid / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D002118:Calcium / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D049452:Green Fluorescent Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D007700:Kinetics; D045727:Metalloexopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D008855:Microscopy, Electron, Scanning; D046529:Microscopy, Electron, Transmission; D008958:Models, Molecular; D058105:Polymerization; D066263:Protein Aggregation, Pathological; D015202:Protein Engineering; D017510:Protein Folding; D054730:Protein Interaction Domains and Motifs; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D020449:Repetitive Sequences, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D000682:Amyloid; D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D000469:Alkaline Phosphatase; C099349:AprP protease, Pseudomonas; D045727:Metalloexopeptidases; C038495:Pseudomonas serine proteinase; D012697:Serine Endopeptidases; D002118:Calcium