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We also demonstrate that, in the periplasm, the only cysteine residue of ZraP is at least partially reduced. Using SAXS, we conclude that the previously determined X-ray structure is different from the structure in solution. Our results allow us to propose a general mechanism for the Zra system activation and to compare it to the homologous Cpx system. We bring new input on the so far poorly described Zra system and notably on ZraS. We bring new input on the so far poorly described Zra system and notably on ZraS.To explore the role of d
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