Biophysical and physiological characterization of ZraP from Escherichia coli, the periplasmic accessory protein of the atypical ZraSR two-component system
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ZraP is an octamer containing four interfacial metal-binding sites contributing to dimer stability. Zinc binding enhances its chaperone properties and zinc-bound ZraP represses the expression of the zraPSR operon. None of the Zra proteins are involved in zinc resistance.
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2018 ◽
Vol 21
(3and4)
◽
pp. 248
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2016 ◽
Vol 120
(49)
◽
pp. 12466-12473
◽
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