title: NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
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.
authors.affiliation: Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.
authors.forename: Michal S
authors.initials: MS
authors.lastname: Shoshan
authors.forename: Deborah E
authors.initials: DE
authors.lastname: Shalev
authors.forename: Wencke
authors.initials: W
authors.lastname: Adriaens
authors.forename: Maarten
authors.initials: M
authors.lastname: Merkx
authors.forename: Tilman M
authors.initials: TM
authors.lastname: Hackeng
authors.forename: Edit Y
authors.initials: EY
authors.lastname: Tshuva
mesh_terms: D003300:Copper / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D056511:Metallochaperones / Q000737:chemistry*; D008715:Methionine / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry; D011485:Protein Binding
chemical_list: D056511:Metallochaperones; D010455:Peptides; D003300:Copper; D008715:Methionine