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Hoyer, Elisabeth; Knöppel, Julius; Liebmann, Martina; Steppert, Michael; Raiwa, Manuel; Herczynski, Olivia; Hanspach, Erik; Zehner, Susanne; Göttfert, Michael; Tsushima, Satoru; Fahmy, Karim; Oertel, Jana

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

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  • Medientyp: E-Artikel
  • Titel: Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity
  • Beteiligte: Hoyer, Elisabeth; Knöppel, Julius; Liebmann, Martina; Steppert, Michael; Raiwa, Manuel; Herczynski, Olivia; Hanspach, Erik; Zehner, Susanne; Göttfert, Michael; Tsushima, Satoru; Fahmy, Karim; Oertel, Jana
  • Erschienen: Springer Science and Business Media LLC, 2019
  • Erschienen in: Scientific Reports
  • Sprache: Englisch
  • DOI: 10.1038/s41598-019-42898-0
  • ISSN: 2045-2322
  • Schlagwörter: Multidisciplinary
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: <jats:title>Abstract</jats:title><jats:p>Strains of the Gram-negative bacterium <jats:italic>Vibrio coralliilyticus</jats:italic> cause the bleaching of corals due to decomposition of symbiotic microalgae. The <jats:italic>V. coralliilyticus</jats:italic> 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 <jats:italic>Bradyrhizobium japonicum</jats:italic> (USDA110). VIC_001052 has been shown to undergo auto-cleavage in the presence of Ca<jats:sup>2+</jats:sup> similar to the NopE proteins. We have studied the hitherto unknown secondary structure, Ca<jats:sup>2+</jats:sup>-binding affinity and stoichiometry of the “metal ion-inducible autocleavage” (MIIA) domain of VIC_001052 which does not possess a classical Ca<jats:sup>2+</jats:sup>-binding motif. CD and fluorescence spectroscopy revealed that the MIIA domain is largely intrinsically disordered. Binding of Ca<jats:sup>2+</jats:sup> and other di- and trivalent cations induced secondary structure and hydrophobic packing after partial neutralization of the highly negatively charged MIIA domain. Mass spectrometry and isothermal titration calorimetry showed two Ca<jats:sup>2+</jats:sup>-binding sites which promote structure formation with a total binding enthalpy of −110 kJ mol<jats:sup>−1</jats:sup> at a low micromolar K<jats:sub>d</jats:sub>. Putative binding motifs were identified by sequence similarity to EF-hand domains and their structure analyzed by molecular dynamics simulations. The stoichiometric Ca<jats:sup>2+</jats:sup>-dependent induction of structure correlated with catalytic activity and may provide a “host-sensing” mechanism that is shared among pathogens that use a T3SS for efficient secretion of disordered proteins.</jats:p>
  • Zugangsstatus: Freier Zugang