A new family of periplasmic-binding proteins that sense arsenic oxyanions
Osborne, Thomas H.
Santini, Joanne M.
MetadataShow full item record
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.
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.-.
PubMed Central IDPMC5908839
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
- The conserved Candida albicans CA3427 gene product defines a new family of proteins exhibiting the generic periplasmic binding protein structural fold.
- Authors: Santini S, Claverie JM, Mouz N, Rousselle T, Maza C, Monchois V, Abergel C
- Issue date: 2011 Apr 11
- Structural basis for high-affinity adipate binding to AdpC (RPA4515), an orphan periplasmic-binding protein from the tripartite tricarboxylate transporter (TTT) family in Rhodopseudomonas palustris.
- Authors: Rosa LT, Dix SR, Rafferty JB, Kelly DJ
- Issue date: 2017 Dec
- A periplasmic arsenite-binding protein involved in regulating arsenite oxidation.
- Authors: Liu G, Liu M, Kim EH, Maaty WS, Bothner B, Lei B, Rensing C, Wang G, McDermott TR
- Issue date: 2012 Jul
- Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA.
- Authors: Lawson DM, Williams CE, Mitchenall LA, Pau RN
- Issue date: 1998 Dec 15
- Structure of a periplasmic glucose-binding protein from Thermotoga maritima.
- Authors: Palani K, Kumaran D, Burley SK, Swaminathan S
- Issue date: 2012 Dec 1