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Gene Review:

cutC - copper homeostasis protein CutC

Escherichia coli O157:H7 str. EDL933

Adaikkalam, V. et al., Roberts, S.A. et al., Zhu, Y.Q. et al., Rensing, C. et al.

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Disease relevance of cutC

Escherichia coli mechanisms of copper homeostasis in a changing environment [1].
We describe an operon, copABCD, that encodes copper-binding and sequestering proteins for copper homeostasis in the copper-sensitive strain Pseudomonas putida PNL-MK25 [2].
Purification and preliminary crystallographic studies of CutC, a novel copper homeostasis protein from Shigella flexneri [3].

High impact information on cutC

The methionine-rich portion of the protein, which is similar to that of other proteins involved in copper homeostasis, does not display additional copper binding [4].
This is the second operon characterized as being involved in copper homeostasis, in addition to a P1-type ATPase encoded by cueAR, which was previously shown to be active in the same strain [2].

References

Escherichia coli mechanisms of copper homeostasis in a changing environment. Rensing, C., Grass, G. FEMS Microbiol. Rev. (2003) [Pubmed]
Characterization of copABCD operon from a copper-sensitive Pseudomonas putida strain. Adaikkalam, V., Swarup, S. Can. J. Microbiol. (2005) [Pubmed]
Purification and preliminary crystallographic studies of CutC, a novel copper homeostasis protein from Shigella flexneri. Zhu, Y.Q., Zhu, D.Y., Lu, H.X., Yang, N., Li, G.P., Wang, D.C. Protein Pept. Lett. (2005) [Pubmed]
A labile regulatory copper ion lies near the T1 copper site in the multicopper oxidase CueO. Roberts, S.A., Wildner, G.F., Grass, G., Weichsel, A., Ambrus, A., Rensing, C., Montfort, W.R. J. Biol. Chem. (2003) [Pubmed]

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