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A new family of periplasmic-binding proteins that sense arsenic oxyanions

DOI: 10.1038/s41598-018-24591-w DOI Help

Authors: Consuelo Pia Badilla (University College London (UCL)) , Thomas H. Osborne (University College Lon) , Ambrose Cole (Birkbeck College, University of London) , Cameron Watson (University College London) , Snezana Djordjevic (University College London) , Joanne M. Santini (University College London (UCL))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Scientific Reports , VOL 8

State: Published (Approved)
Published: April 2018
Diamond Proposal Number(s): 9204

Open Access Open Access

Abstract: 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.

Journal Keywords: Biochemistry; Microbiology

Subject Areas: Biology and Bio-materials, Chemistry

Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: Soleil


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