Model peptide studies of Ag+ binding sites from the silver resistance protein SilEElectronic supplementary information (ESI) available: Experimental details, binding constant determination, NMR spectra, methionine oxidation assays, and silver-methionine crystal structure. CCDC 1547635. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c7cc02630g

• Main Authors: Chabert, V, Hologne, M, Sénèque, O, Crochet, A, Walker, O, Fromm, K. M
• Format: Article
• Language: English
• ISSN: 1359-7345; 1364-548X
• DOI: 10.1039/c7cc02630g

Using model peptides, each of the nine MX 2 H or HX n M ( n = 1, 2) motifs of the silver resistance protein SilE has been shown to coordinate to one Ag + ion by its histidine and methionine residues with K d in the μM range. This suggests an Ag + buffering role for SilE in the case of high Ag + overload. A model peptide study characterizes several Ag + -binding sites of the bacterial silver resistant protein SilE, providing new insights into its physiological role.