Structure and Metal binding Characterization of the C-terminal Mellochaperone Domain of Membrane Fusion Protein SilB from Cupriavidus metallidurans CH34

Research output: Contribution to journalArticle

Authors

  • Beate Bersch
  • Kheiro-mouna Derfoufi
  • Fabien de Angelis
  • Vanessa Auquier
  • Elisabeth Ngonlong Ekende
  • Max Mergeay
  • Jean-Marie Ruysschaert
  • Guy Vandenbussche

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DOI

Abstract

In Cupriavidus metallidurans CH34, a model organism for heavy metal resistance studies, the sil determinant is potentially involved in the efflux of of silver and copper ions. Proteins SilA, SilB, SilC form a resistance/nodulation/cell division (RND)-based transport system in which SilB is the periplasmic adaptor protein belonging to the membrane fusion protein family. In addition sto the four domains typical of known MFPs, SilB has a fifth additional C-terminal domain , SilB440-521. Structure and backbone of SilB440-521 have been investigated using NMR, and the residues of the metal site have been from 15N- and 13C-edited HSQC spectra.The solution structure and additional metal binding experiments that this C-terminal domain folds independantly of the rest of the protein and has a conformation and a Ag+ /Cu+ binding specificity similar to those determined for CusF from Escherichia coli. The samll protein CusF plays a role in metal trafficking in the periplasm. This suggests a potential metallochaperone role for SilB440-521 that is discussed in the context of simultaneous expression of different determinants involved in copper resistance in C.metallidurans CH34

Details

Original languageEnglish
Pages (from-to)2194-2204
JournalBiochemistry
Volume50
Issue number12
DOIs
Publication statusPublished - 7 Feb 2011

Keywords

  • Cupriavidus metallidurans, resistance to silver, copper, SilB Membrane Fusion protein, efflux, structure, metallochaperone, NMR, HSQC spectra

ID: 123700