Abstract
ArsD is a metallochaperone that delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773. Conserved ArsD cysteine residues (Cys12, Cys13 and Cys18) construct the As(III) binding site of the protein, however a global structural understanding of this arsenic binding remains unclear. We have obtained NMR assignments for ArsD as a starting point for probing structural changes on the protein that occur in response to metalloid binding and upon formation of a complex with ArsA. The predicted solution structure of ArsD is in agreement with recently published crystallographic structural results.
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Acknowledgments
We thank the National High Magnetic Field Laboratory (NHMFL) in Tallahassee, FL. for 720 MHz NMR time as part of their user’s program. The INOVA 600 MHz spectrometer with cold probe was purchased through NIH support (1S10RR16626-01). The work was supported by NIH grants AI043428 (BPR) and DK068139 (TLS).
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Ye, J., He, Y., Skalicky, J. et al. Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution. Biomol NMR Assign 5, 109–112 (2011). https://doi.org/10.1007/s12104-010-9279-9
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DOI: https://doi.org/10.1007/s12104-010-9279-9