Model peptide studies of Ag+ binding sites from the silver resistance protein SilE

V Chabert; M Hologne; O Sénèque; A Crochet; O Walker; K M Fromm

doi:10.1039/c7cc02630g

Model peptide studies of Ag⁺ binding sites from the silver resistance protein SilE

Chem Commun (Camb). 2017 Jun 1;53(45):6105-6108. doi: 10.1039/c7cc02630g.

Authors

V Chabert¹, M Hologne, O Sénèque, A Crochet, O Walker, K M Fromm

Affiliation

¹ Univ. Fribourg, Department of Chemistry, Chemin du Musée 9, 1700 Fribourg, Switzerland. katharina.fromm@unifr.ch.

PMID: 28530293
DOI: 10.1039/c7cc02630g

Abstract

Using model peptides, each of the nine MX₂H or HX_nM (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.

MeSH terms

Bacterial Proteins / chemistry
Bacterial Proteins / metabolism*
Binding Sites
Carrier Proteins / chemistry
Carrier Proteins / metabolism*
Drug Resistance, Bacterial / physiology
Glutamic Acid / chemistry
Glutamic Acid / metabolism
Histidine / chemistry
Histidine / metabolism
Methionine / chemistry
Methionine / metabolism
Peptide Fragments / chemical synthesis
Peptide Fragments / chemistry
Peptide Fragments / metabolism*
Protein Binding
Silver / chemistry
Silver / metabolism*

Substances

Bacterial Proteins
Carrier Proteins
Peptide Fragments
Glutamic Acid
Silver
Histidine
Methionine