A new family of periplasmic-binding proteins that sense arsenic oxyanions
Authors
Badilla, ConsueloOsborne, Thomas H.
Cole, Ambrose
Watson, Cameron
Djordjevic, Snezana
Santini, Joanne M.
Issue Date
2018-04-19
Metadata
Show full item recordAbstract
Arsenic contamination of drinking water affects more than 140 million people worldwide. While toxic to humans, inorganic forms of arsenic (arsenite and arsenate), can be used as energy sources for microbial respiration. AioX and its orthologues (ArxX and ArrX) represent the first members of a new sub-family of periplasmic-binding proteins that serve as the first component of a signal transduction system, that’s role is to positively regulate expression of arsenic metabolism enzymes. As determined by X-ray crystallography for AioX, arsenite binding only requires subtle conformational changes in protein structure, providing insights into protein-ligand interactions. The binding pocket of all orthologues is conserved but this alone is not sufficient for oxyanion selectivity, with proteins selectively binding either arsenite or arsenate. Phylogenetic evidence, clearly demonstrates that the regulatory proteins evolved together early in prokaryotic evolution and had a separate origin from the metabolic enzymes whose expression they regulate.Citation
Badilla C, Osborne TH, Cole A, Watson C, Djordjevic S, Santini JM (2018) 'A new family of periplasmic-binding proteins that sense arsenic oxyanions', Scientific Reports, 8 (6282), pp.-.Publisher
SpringerNatureJournal
Scientific ReportsPubMed ID
29674678PubMed Central ID
PMC5908839Additional Links
https://www.nature.com/articles/s41598-018-24591-wType
ArticleLanguage
enISSN
2045-2322ae974a485f413a2113503eed53cd6c53
10.1038/s41598-018-24591-w
Scopus Count
Collections
The following license files are associated with this item:
- Creative Commons
Except where otherwise noted, this item's license is described as Green - can archive pre-print and post-print or publisher's version/PDF