9RCM
Laccase (multicopper oxidase) from Pediococcus pentosaceus 4618 mutant E451L co-crystallized with Copper Chloride
9RCM の概要
| エントリーDOI | 10.2210/pdb9rcm/pdb |
| 関連するPDBエントリー | 9RC5 |
| 分子名称 | Multicopper oxidase domain-containing protein, COPPER (II) ION, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | laccase, oxidoreductase, multicopper oxidase |
| 由来する生物種 | Pediococcus pentosaceus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 60187.81 |
| 構造登録者 | |
| 主引用文献 | Gasco, R.,Sendra, R.,Olmeda, I.,Paredes-Martinez, F.,Ferrer, S.,Pardo, I.,Casino, P. Laccases from lactic acid bacteria show cuprous oxidase activity and capture Cu(II) and Ag(I) ions. Protein Sci., 35:e70385-e70385, 2026 Cited by PubMed Abstract: Several laccases derived from lactic acid bacteria (LAB) display specific structural features, such as two methionine residues at the entrance of the T1Cu center, and an extended C-terminal end enriched in methionine and histidine. To investigate their functional roles, we engineered mutant variants of the laccase Pp4816 from Pediococcus pentosaceus and analyzed them using both functional and structural approaches. We identified a cuprous oxidase activity that is essential for the oxidation of 2,6-dimethoxyphenol (2,6-DMP) and other substrates, but dispensable for ABTS. The two Met residues at the entrance of the T1Cu center are crucial for this activity while the C-terminus has a minor impact and shows conformational flexibility. Through anomalous diffraction studies, we located Cu(II) bound at the entrance of the T1Cu center and additional surface sites, and demonstrated that Ag(I) acts as an inhibitor of the cuprous oxidase activity, which binds to overlapping positions, including the C-terminus. This cuprous oxidase activity was found to be conserved in other laccases from LAB, suggesting that these enzymes function as copper and silver chelators with potential biotechnological applications, such as environmental copper detoxification. PubMed: 41432273DOI: 10.1002/pro.70385 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






