3PGB
Crystal structure of Aspergillus nidulans amine oxidase
3PGB の概要
| エントリーDOI | 10.2210/pdb3pgb/pdb |
| 分子名称 | Putative uncharacterized protein, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| 機能のキーワード | oxidoreductase, copper amine oxidase, cao, topaquinone, tpq |
| 由来する生物種 | Emericella nidulans (Aspergillus nidulans) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 92629.38 |
| 構造登録者 | |
| 主引用文献 | McGrath, A.P.,Mithieux, S.M.,Collyer, C.A.,Bakhuis, J.G.,van den Berg, M.,Sein, A.,Heinz, A.,Schmelzer, C.,Weiss, A.S.,Guss, J.M. Structure and Activity of Aspergillus nidulans Copper Amine Oxidase Biochemistry, 50:5718-5730, 2011 Cited by PubMed Abstract: Aspergillus nidulans amine oxidase (ANAO) has the unusual ability among the family of copper and trihydroxyphenylalanine quinone-containing amine oxidases of being able to oxidize the amine side chains of lysine residues in large peptides and proteins. We show here that in common with the related enzyme from the yeast Pichia pastoris, ANAO can promote the cross-linking of tropoelastin and oxidize the lysine residues in α-casein proteins and tropoelastin. The crystal structure of ANAO, the first for a fungal enzyme in this family, has been determined to a resolution of 2.4 Å. The enzyme is a dimer with the archetypal fold of a copper-containing amine oxidase. The active site is the most open of any of those of the structurally characterized enzymes in the family and provides a ready explanation for its lysine oxidase-like activity. PubMed: 21604787DOI: 10.1021/bi200555c 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.45 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






