Structure and Function of the Engineered Multicopper Oxidase , CueO from Escherichia coli ⎯ Deletion of the Methionine - Rich Helical Region Covering the Substrate
نویسندگان
چکیده
*KURAに登録されているコンテンツの利用については,著作権法に規定されている私的使用や引用などの範囲内で行ってください。 *著作権法に規定されている私的使用や引用などの範囲を超える利用を行う場合には,著作権者の許諾を得てください。ただし,著作権者 から著作権等管理事業者(学術著作権協会,日本著作出版権管理システムなど)に権利委託されているコンテンツの利用手続については ,各著作権等管理事業者に確認してください。 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(s) Kataoka, Kunishige; Komori, Hirofumi; Ueki, Yusaku; Konno, Yusuke; Kamitaka, Yuji; Kurose, Shinji; Tsujimura, Seiya; Higuchi, Yoshiki; Kano, Kenji; Seo, Daisuke; Sakurai, Takeshi Citation Journal of Molecular Biology, 373(1): 141-152
منابع مشابه
Structure and function of the engineered multicopper oxidase CueO from Escherichia coli--deletion of the methionine-rich helical region covering the substrate-binding site.
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-His40...
متن کاملThe functional roles of the three copper sites associated with the methionine-rich insert in the multicopper oxidase CueO from E. coli.
CueO from Escherichia coli is a multicopper oxidase (MCO) involved in copper tolerance under aerobic conditions. It features the four typical copper atoms that act as electron transfer (T1) and dioxygen reduction (T2, T3; trinuclear) sites. In addition, it displays a methionine- and histidine-rich insert that includes a helix that blocks physical access to the T1 site. In crystalline form, the ...
متن کاملLinkage between catecholate siderophores and the multicopper oxidase CueO in Escherichia coli.
The multicopper oxidase CueO had previously been demonstrated to exhibit phenoloxidase activity and was implicated in intrinsic copper resistance in Escherichia coli. Catecholates can potentially reduce Cu(II) to the prooxidant Cu(I). In this report we provide evidence that CueO protects E. coli cells by oxidizing enterobactin, the catechol iron siderophore of E. coli, in the presence of copper...
متن کاملTrade-off between iron uptake and protection against oxidative stress: deletion of cueO promotes uropathogenic Escherichia coli virulence in a mouse model of urinary tract infection.
The periplasmic multicopper oxidase (CueO) is involved in copper homeostasis and protection against oxidative stress. Here, we show that the deletion of cueO in uropathogenic Escherichia coli increases its colonization of the urinary tract despite its increased sensitivity to hydrogen peroxide. The cueO deletion mutant accumulated iron with increased efficiency compared to its parent strain; th...
متن کاملA robust metallo-oxidase from the hyperthermophilic bacterium Aquifex aeolicus.
The gene, Aquifex aeolicus AAC07157.1, encoding a multicopper oxidase (McoA) and localized in the genome as part of a putative copper-resistance determinant, has been cloned, over-expressed in Escherichia coli and the recombinant enzyme purified to homogeneity. The purified enzyme shows spectroscopic and biochemical characteristics typical of the well-characterized multicopper oxidase family of...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2017