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

2.50
Hdl Handle:
http://hdl.handle.net/10547/622798
Title:
A new family of periplasmic-binding proteins that sense arsenic oxyanions
Authors:
Badilla, Consuelo; Osborne, Thomas H.; Cole, Ambrose; Watson, Cameron; Djordjevic, Snezana ( 0000-0002-6699-8083 ) ; Santini, Joanne M. ( 0000-0003-1808-898X )
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.
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:
SpringerNature
Journal:
Scientific Reports
Issue Date:
19-Apr-2018
URI:
http://hdl.handle.net/10547/622798
DOI:
10.1038/s41598-018-24591-w
PubMed Central ID:
PMC5908839
Additional Links:
https://www.nature.com/articles/s41598-018-24591-w
Type:
Article
Language:
en
ISSN:
2045-2322
Appears in Collections:
Biomedical and biological science

Full metadata record

DC FieldValue Language
dc.contributor.authorBadilla, Consueloen
dc.contributor.authorOsborne, Thomas H.en
dc.contributor.authorCole, Ambroseen
dc.contributor.authorWatson, Cameronen
dc.contributor.authorDjordjevic, Snezanaen
dc.contributor.authorSantini, Joanne M.en
dc.date.accessioned2018-07-10T12:54:21Z-
dc.date.available2018-07-10T12:54:21Z-
dc.date.issued2018-04-19-
dc.identifier.citationBadilla 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.-.en
dc.identifier.issn2045-2322-
dc.identifier.doi10.1038/s41598-018-24591-w-
dc.identifier.urihttp://hdl.handle.net/10547/622798-
dc.description.abstractArsenic 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.en
dc.language.isoenen
dc.publisherSpringerNatureen
dc.relation.urlhttps://www.nature.com/articles/s41598-018-24591-wen
dc.rightsGreen - can archive pre-print and post-print or publisher's version/PDF-
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/*
dc.subjectwater qualityen
dc.subjectarsenicen
dc.subjectperiplasmic-binding proteinsen
dc.titleA new family of periplasmic-binding proteins that sense arsenic oxyanionsen
dc.typeArticleen
dc.identifier.journalScientific Reportsen
dc.identifier.pmcidPMC5908839-
dc.date.updated2018-07-10T12:50:44Z-
dc.description.noteopen access article with cc licence RVO 10/7/18-
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