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September 10, 2025Proceedings of the National Academy of SciencesOpen Access

Nucleotide- and metalloid-driven conformational changes in the arsenite efflux ATPase ArsA

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Authors

SMShivansh MahajanAPAshley E. PallYLYancheng E. Li

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Overview

This study reveals how arsenite and nucleotides influence ArsA function, suggesting significant implications for prokaryotic resistance.

Key Points

  • Conformational changes in ArsA are driven by nucleotide binding and modulate arsenite efflux mechanisms.
  • Cryogenic electron microscopy structures show open and closed states of ArsA bound to ADP, ATP, and arsenite.
  • X-ray absorption spectroscopy confirmed binding of arsenite at the catalytic site, critical for ArsA function.
  • This research provides insights into the role of nucleotide hydrolysis in arsenite resistance in prokaryotes.

Cite This Study

Mahajan et al. (2025) studied this question.

synapsesocial.com/papers/68c1d7f654b1d3bfb60fa265https://doi.org/10.1073/pnas.2506440122
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