Selectivity in heavy metal-binding to peptides and proteins

Tara M. DeSilva, Gianluigi Veglia, Fernando Porcelli, Andrew M. Prantner, Stanley J. Opella

Research output: Contribution to journalArticlepeer-review

81 Scopus citations

Abstract

The metal-binding affinities and three-dimensional structures of three synthetic 18-residue peptides with sequences derived from that of the highly conserved metal-binding motif MXCXXC found in many heavy metal-binding proteins were determined. A change in register of the cysteines and alanines of the sequence from the periplasmic mercury-binding protein, MerP, i.e., CAAC, CACA, and CCAA, affects the specificity of metal binding, in particular, the peptide with vicinal cysteines binds only mercury. The three-dimensional structures of the mercury-bound forms of the three peptides determined in solution by NMR spectroscopy peptides differ considerably, even though they are all linear bicoordinate complexes. The three-dimensional structure of the peptide with CAAC bound to Cd(II) demonstrates that the metal-binding loop is malleable enough to accommodate modes of coordination other than linear bicoordinate.

Original languageEnglish (US)
Pages (from-to)189-197
Number of pages9
JournalBiopolymers
Volume64
Issue number4
DOIs
StatePublished - Aug 5 2002

Keywords

  • Cadmium
  • Mercury
  • Mercury-binding protein
  • NMR spectroscopy
  • Peptides

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