SilE is an intrinsically disordered periplasmic "molecular sponge" involved in bacterial silver resistance.
Mol Microbiol
; 101(5): 731-42, 2016 09.
Article
en En
| MEDLINE
| ID: mdl-27085056
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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Salmonella typhimurium
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Plata
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Proteínas Bacterianas
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Proteínas Portadoras
Tipo de estudio:
Prognostic_studies
Idioma:
En
Año:
2016
Tipo del documento:
Article