Structural properties of the Caulobacter crescentus copper resistance protein, PcoB
Copper cations play fundamental roles in biological systems, such as in folding and stabilizing proteins, or in enzyme reactions. While essential to the proper functioning of cells, copper in too high concentration can become toxic to them, and organisms have therefore developed tight regulatory mechanisms towards these cations. For instance, the Pco system found in the Caulobacter crescentus bacterium, is composed of two proteins: a soluble periplasmic protein PcoA and an outer membrane protein PcoB. PcoA oxidizes Cu+ to Cu2+, and PcoB is thought to be an efflux pump for these divalent cations. Whilst the PcoA protein has already been studied, much less is known about PcoB structure and function. In the present project, we plan to understand the structural properties of the native PcoB, and to validate its refolding by a peculiar method based on the association of sodium dodecyl sulfate (SDS) and 2-methylpentane-2,4-diol (MPD). First, the native PcoB extracted from the Caulobacter crescentus membrane will be studied while solubilized using the match-out deuterated N-Dodecyl-Beta-D-Maltoside. Then the refolding of the d-SDS denatured protein by adding d-MPD will be monitored.
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The recommended format for citing this dataset in a research publication is in the following format:
MICHAUX Catherine; HENNAUX Laurelenn and MARTEL Anne. (2023). Structural properties of the Caulobacter crescentus copper resistance protein, PcoB. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1077
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This data is not yet public
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