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

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

Chem Commun (Camb) ; 53(45): 6105-6108, 2017 Jun 01.

Article in English | MEDLINE | ID: mdl-28530293

ABSTRACT

Using model peptides, each of the nine MX2H or HXnM (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 Kd in the µM range. This suggests an Ag+ buffering role for SilE in the case of high Ag+ overload.

Subject(s)

Bacterial Proteins/metabolism , Carrier Proteins/metabolism , Peptide Fragments/metabolism , Silver/metabolism , Bacterial Proteins/chemistry , Binding Sites , Carrier Proteins/chemistry , 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 , Protein Binding , Silver/chemistry

ABSTRACT

Subject(s)

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