Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity.

ABSTRACT: Strains of the Gram-negative bacterium Vibrio coralliilyticus cause the bleaching of corals due to decomposition of symbiotic microalgae. The V. coralliilyticus strain ATCC BAA-450 (Vc450) encodes a type III secretion system (T3SS). The gene cluster also encodes a protein (locus tag VIC_001052) with sequence homology to the T3SS-secreted nodulation proteins NopE1 and NopE2 of Bradyrhizobium japonicum (USDA110). VIC_001052 has been shown to undergo auto-cleavage in the presence of Ca²⁺ similar to the NopE proteins. We have studied the hitherto unknown secondary structure, Ca²⁺-binding affinity and stoichiometry of the "metal ion-inducible autocleavage" (MIIA) domain of VIC_001052 which does not possess a classical Ca²⁺-binding motif. CD and fluorescence spec

SUBMITTER: Hoyer E 

PROVIDER: S-EPMC6506597 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature