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

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

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Arsenic / metabolism*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Metallochaperones / chemistry*
  • Molecular Chaperones / chemistry*
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Solutions

Substances

  • ArsD protein, E coli
  • Escherichia coli Proteins
  • Metallochaperones
  • Molecular Chaperones
  • Solutions
  • Arsenic