Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.

@article{Kataoka2007StructureAF,
  title={Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.},
  author={Kunimitsu Kataoka and Hirofumi Komori and Yusaku Ueki and Yusuke Konno and Yuji Kamitaka and Shinji Kurose and Seiya Tsujimura and Yoshiki Higuchi and Kenji Kano and Daisuke Seo and Takeshi Sakurai},
  journal={Journal of molecular biology},
  year={2007},
  volume={373 1},
  pages={
          141-52
        }
}
CueO is a multicopper oxidase (MCO) that is involved in the homeostasis of Cu in Escherichia coli and is the sole cuprous oxidase to have ever been found. Differing from other MCOs, the substrate-binding site of CueO is deeply buried under a methionine-rich helical region including alpha-helices 5, 6, and 7 that interfere with the access of organic substrates. We deleted the region Pro357-His406 and replaced it with a Gly-Gly linker. The crystal structures of a truncated mutant in the presence… CONTINUE READING

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