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Structure and Function of the Engineered Multicopper Oxidase CueO from Escherichia coli-Deletion of the Methionine-Rich Helical Region Covering the Substrate-Binding Site
http://hdl.handle.net/2297/7110
http://hdl.handle.net/2297/71107b47eece-9e3c-44cc-9f45-10c0bbda203e
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
SC-PR-SAKURAI-T-141.pdf (1.1 MB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-10-03 | |||||
| タイトル | ||||||
| タイトル | Structure and Function of the Engineered Multicopper Oxidase CueO from Escherichia coli-Deletion of the Methionine-Rich Helical Region Covering the Substrate-Binding Site | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
Kataoka, Kunishige
× Kataoka, Kunishige× Komori, Hirofumi× Ueki, Yusaku× Konno, Yusuke× Kamitaka, Yuji× Kurose, Shinji× Tsujimura, Seiya× Higuchi, Yoshiki× Kano, Kenji× Seo, Daisuke× Sakurai, Takeshi |
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| 提供者所属 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 金沢大学大学院自然科学研究科物質創成 | |||||
| 提供者所属 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 金沢大学理学部 | |||||
| 書誌情報 |
Journal of Molecular Biology 巻 373, 号 1, p. 141-152, 発行日 2007-10-12 |
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| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0022-2836 | |||||
| NCID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA00702794 | |||||
| DOI | ||||||
| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1016/j.jmb.2007.07.041 | |||||
| 出版者 | ||||||
| 出版者 | Elsevier | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | 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 α-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 and in the absence of excess Cu(II) indicated that the scaffold of the CueO molecule and metal-binding sites were reserved in comparison with those of CueO. In addition, the high thermostability of the protein molecule and its spectroscopic and magnetic properties due to four Cu centers were also conserved after truncation. As for functions, the cuprous oxidase activity of the mutant was reduced to ca 10% that of recombinant CueO owing to the decrease in the affinity of the labile Cu site for Cu(I) ions, although activities for laccase substrates such as 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), p-phenylenediamine, and 2,6-dimethoxyphenol increased due to changes in the access of these organic substrates to the type I Cu site. The present engineering of CueO indicates that the methionine-rich α-helices function as a barrier to the access of bulky organic substrates, which provides CueO with specificity as a cuprous oxidase. © 2007 Elsevier Ltd. All rights reserved. | |||||
| 著者版フラグ | ||||||
| 出版タイプ | AM | |||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
