NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine

Chem Commun (Camb). 2011 Jun 14;47(22):6407-9. doi: 10.1039/c1cc11600b. Epub 2011 May 9.

Abstract

The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and ∼6.8 Cu(I) binds through one Cys and the Met rather than the two Cys residues, differently than at pH ∼8.5. This suggests a possible role of Met in metal transport.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Copper / chemistry*
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy
  • Metallochaperones / chemistry*
  • Methionine / chemistry
  • Methionine / physiology*
  • Models, Molecular
  • Peptides / chemistry
  • Protein Binding

Substances

  • Metallochaperones
  • Peptides
  • Copper
  • Methionine