4EF3
Multicopper Oxidase CueO (Citrate buffer)
4EF3 の概要
| エントリーDOI | 10.2210/pdb4ef3/pdb |
| 分子名称 | Blue copper oxidase CueO, COPPER (II) ION, HYDROXIDE ION, ... (6 entities in total) |
| 機能のキーワード | multicopper oxidase, metal binding protein |
| 由来する生物種 | Escherichia coli |
| 細胞内の位置 | Periplasm: P36649 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 54019.65 |
| 構造登録者 | Komori, H.,Kataoka, K.,Sakurai, T.,Higuchi, Y. (登録日: 2012-03-29, 公開日: 2013-05-22, 最終更新日: 2024-03-20) |
| 主引用文献 | Komori, H.,Kataoka, K.,Tanaka, S.,Matsuda, N.,Higuchi, Y.,Sakurai, T. Exogenous acetate ion reaches the type II copper centre in CueO through the water-excretion channel and potentially affects the enzymatic activity. Acta Crystallogr.,Sect.F, 72:558-563, 2016 Cited by PubMed Abstract: The acetate-bound form of the type II copper was found in the X-ray structure of the multicopper oxidase CueO crystallized in acetate buffer in addition to the conventional OH(-)-bound form as the major resting form. The acetate ion was retained bound to the type II copper even after prolonged exposure of a CueO crystal to X-ray radiation, which led to the stepwise reduction of the Cu centres. However, in this study, when CueO was crystallized in citrate buffer the OH(-)-bound form was present exclusively. This fact shows that an exogenous acetate ion reaches the type II Cu centre through the water channel constructed between domains 1 and 3 in the CueO molecule. It was also found that the enzymatic activity of CueO is enhanced in the presence of acetate ions in the solvent water. PubMed: 27380373DOI: 10.1107/S2053230X16009237 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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