Journal article

Structural and Functional Investigation of the Periplasmic Arsenate-Binding Protein ArrX from Chrysiogenes arsenatis

Nilakhi Poddar, Consuelo Badilla, Shadi Maghool, Thomas H Osborne, Joanne M Santini, Megan J Maher

BIOCHEMISTRY | AMER CHEMICAL SOC | Published : 2021

Abstract

The anaerobic bacterium Chrysiogenes arsenatis respires using the oxyanion arsenate (AsO43-) as the terminal electron acceptor, where it is reduced to arsenite (AsO33-) while concomitantly oxidizing various organic (e.g., acetate) electron donors. This respiratory activity is catalyzed in the periplasm of the bacterium by the enzyme arsenate reductase (Arr), with expression of the enzyme controlled by a sensor histidine kinase (ArrS) and a periplasmic-binding protein (PBP), ArrX. Here, we report for the first time, the molecular structure of ArrX in the absence and presence of bound ligand arsenate. Comparison of the ligand-bound structure of ArrX with other PBPs shows a high level of conser..

View full abstract

Grants

Awarded by Australian Research Council (ARC) Future Fellowship


Awarded by Biotechnology and Biological Sciences Research Council (BBSRC)


Funding Acknowledgements

This research was funded by an Australian Research Council (ARC) Future Fellowship to M.J.M. (FT180100397) and a Biotechnology and Biological Sciences Research Council (BBSRC) grant (BB/N012674/1) to J.M.S. N.P. was supported by a University of Melbourne Research Scholarship, and C.B. was supported by a studentship provided by CONICYT, Chile.