1IVX

Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.

1IVX の概要

• エントリーDOI: 10.2210/pdb1ivx/pdb
• 関連するPDBエントリー: 1AV4 1AVK 1AVL 1IQX 1IQY 1IU7 1IVU 1IVV 1IVW
• 分子名称: amine oxidase, COPPER (II) ION (3 entities in total)
• 機能のキーワード: oxidoreductase, copper, amine oxidase, biogenesis, tpq, freeze-trapp, intermediate, quinone cofactor
• 由来する生物種: Arthrobacter globiformis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 141632.58

構造登録者

Kim, M.,Okajima, T.,Kishishita, S.,Yoshimura, M.,Kawamori, A.,Tanizawa, K.,Yamaguchi, H. (登録日: 2002-03-29, 公開日: 2002-08-07, 最終更新日: 2023-12-27)

主引用文献

Kim, M.,Okajima, T.,Kishishita, S.,Yoshimura, M.,Kawamori, A.,Tanizawa, K.,Yamaguchi, H.
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
Nat.Struct.Biol., 9:591-596, 2002

PubMed Abstract: The quinone cofactor TPQ in copper amine oxidase is generated by posttranslational modification of an active site tyrosine residue. Using X-ray crystallography, we have probed the copper-dependent autooxidation process of TPQ in the enzyme from Arthrobacter globiformis. Apo enzyme crystals were anaerobically soaked with copper; the structure determined from this crystal provides a view of the initial state: the unmodified tyrosine coordinated to the bound copper. Exposure of the copper-bound crystals to oxygen led to the formation of freeze-trapped intermediates; structural analyses indicate that these intermediates contain dihydroxyphenylalanine quinone and trihydroxyphenylalanine. These are the first visualized intermediates during TPQ biogenesis in copper amine oxidase.

PubMed: 12134140
DOI: 10.1038/nsb824

実験手法

X-RAY DIFFRACTION (2.2 Å)