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. 2011 Apr;5(1):109-12.
doi: 10.1007/s12104-010-9279-9. Epub 2010 Nov 10.

Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution

Jun Ye  1 , Yanan He, Jack Skalicky, Barry P Rosen, Timothy L Stemmler
Affiliations

Resonance assignments and secondary structure prediction of the As(III) metallochaperone ArsD in solution

Jun Ye et al. Biomol NMR Assign. 2011 Apr.

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 (Cys(12), Cys(13) and Cys(18)) 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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Figures

Fig. 1
Fig. 1
Assigned 1H,15N TROSY HSQC spectrum of ArsD. Data were collected on the National Magnet Laboratory’s Varian INOVA 720 MHz spectrometer at 293 K
Fig. 2
Fig. 2
Summary of proposed secondary structural elements for ArsD in solution (middle) compared with structural characterization obtained from crystallographic analysis (bottom) from CSI analysis using NMRView (Johnson 2004). Single letter residue designations are provided (top) with predicted secondary structural elements displayed in red (helix), blue (strand) or grey (unfolded)
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