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

Sci Rep. 2019-05; 
HoyerElisabeth,Kn?ppelJulius,LiebmannMartina,SteppertMichael,RaiwaManuel,HerczynskiOlivia,HanspachErik,ZehnerSusanne,G?ttfertMichael,TsushimaSatoru,FahmyKarim,Oertel
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Recombinant Proteins Anti-DYKDDDDK (FLAG?) G1 Affinity Resin; GenScript (Piscataway Township, USA) was used for purification of FLAG-tagged proteins according to the manufacturer’s protocol. Get A Quote

摘要

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 Ca similar to the NopE proteins. We have studied the hitherto unknown secondary structure, Ca-binding affinity and stoichiometry of the "metal ion-inducible autocleavage" (MIIA) domain of VIC_001052 which does not possess a classical... More

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