@article { , title = {SilE is an intrinsically disordered periplasmic ‘molecular sponge' involved in bacterial silver resistance}, abstract = {Ag+ resistance was initially found on the Salmonella enetrica serovar Typhimurium multi-resistance plasmid pMG101 from burns patients in 1975. The putative model of Ag+ resistance, encoded by the sil operon from pMG101, involves export of Ag+ via an ATPase (SilP), an effluxer complex (SilCFBA) and a periplasmic chaperon of Ag+ (SilE). SilE is predicted to be intrinsically disordered. We tested this hypothesis using structural and biophysical studies and show that SilE is an intrinsically disordered protein in its free apo-form but folds to a compact structure upon optimal binding to six Ag+ ions in its holo-form. Sequence analyses and site-directed mutagenesis established the importance of histidine and methionine containing motifs for Ag+-binding, and identified a nucleation core that initiates Ag+-mediated folding of SilE. We conclude that SilE is a molecular sponge for absorbing metal ions.}, doi = {10.1111/mmi.13399}, eissn = {1365-2958}, issn = {0950-382X}, issue = {5}, journal = {Molecular Microbiology}, note = {Now OA so PDF replaced, visibility changed and set statement removed. HK, 11.08.2016}, pages = {731-742}, publicationstatus = {Published}, publisher = {Wiley}, url = {https://nottingham-repository.worktribe.com/output/790929}, volume = {101}, year = {2016}, author = {Asiani, Karishma R. and Williams, Huw Edward Llewelyn and Bird, Louise and Jenner, Matthew and Searle, Mark S. and Hobman, Jon L. and Scott, David J. and Soultanas, Panos} }