Article
Mutation in the β-hairpin of the Bordetella pertussis adenylate cyclase toxin modulates N-lobe conformation in calmodulin.
Biochemical and biophysical research communications - 10 Oct 2014
Springer Tzvia I, Goebel Erich, Hariraju Dinesh, Finley Natosha L
Abstract excerpt
Bordetella pertussis, causative agent of whooping cough, produces an adenylate cyclase toxin (CyaA) that is an important virulence factor. In the host cell, the adenylate cyclase domain of CyaA (CyaA-ACD) is activated upon association with calmodulin (CaM), an EF-hand protein comprised of N- and C-lobes (N-CaM and C-CaM, respectively) connected by a flexible tether. Maximal CyaA-ACD activation is achieved through...
Topics
- Adenylate Cyclase Toxin
- Amino Acid Substitution
- Binding Sites
- Bordetella pertussis
- Calmodulin
- Host-Pathogen Interactions
- Humans
- Models, Molecular
- Molecular Conformation
- Multiprotein Complexes