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

Download statistics - Document (COUNTER):

Hoyer, E.; Knöppel, J.; Liebmann, M.; Steppert, M.; Raiwa, M. et al.: Calcium binding to a disordered domain of a type III-secreted protein from a coral pathogen promotes secondary structure formation and catalytic activity. In: Scientific Reports 9 (2019), Nr. 1, 7115. DOI: https://doi.org/10.1038/s41598-019-42898-0

Repository version

To cite the version in the repository, please use this identifier: https://doi.org/10.15488/5060

Selected time period:

year: 
month: 

Sum total of downloads: 53




Thumbnail
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 Ca 2+ similar to the NopE proteins. We have studied the hitherto unknown secondary structure, Ca 2+ -binding affinity and stoichiometry of the “metal ion-inducible autocleavage” (MIIA) domain of VIC_001052 which does not possess a classical Ca 2+ -binding motif. CD and fluorescence spectroscopy revealed that the MIIA domain is largely intrinsically disordered. Binding of Ca 2+ 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 2+ -binding sites which promote structure formation with a total binding enthalpy of −110 kJ mol −1 at a low micromolar K d . Putative binding motifs were identified by sequence similarity to EF-hand domains and their structure analyzed by molecular dynamics simulations. The stoichiometric Ca 2+ -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.
License of this version: CC BY 4.0 Unported
Document Type: article
Publishing status: publishedVersion
Issue Date: 2019
Appears in Collections:Fakultät für Mathematik und Physik

distribution of downloads over the selected time period:

downloads by country:

pos. country downloads
total perc.
1 image of flag of Germany Germany 45 84.91%
2 image of flag of United States United States 3 5.66%
3 image of flag of No geo information available No geo information available 1 1.89%
4 image of flag of Russian Federation Russian Federation 1 1.89%
5 image of flag of Korea, Republic of Korea, Republic of 1 1.89%
6 image of flag of India India 1 1.89%
7 image of flag of Egypt Egypt 1 1.89%

Further download figures and rankings:


Hinweis

Zur Erhebung der Downloadstatistiken kommen entsprechend dem „COUNTER Code of Practice for e-Resources“ international anerkannte Regeln und Normen zur Anwendung. COUNTER ist eine internationale Non-Profit-Organisation, in der Bibliotheksverbände, Datenbankanbieter und Verlage gemeinsam an Standards zur Erhebung, Speicherung und Verarbeitung von Nutzungsdaten elektronischer Ressourcen arbeiten, welche so Objektivität und Vergleichbarkeit gewährleisten sollen. Es werden hierbei ausschließlich Zugriffe auf die entsprechenden Volltexte ausgewertet, keine Aufrufe der Website an sich.

Search the repository


Browse