2CG0

AGAO in complex with wc9a (Ru-wire inhibitor, 9-carbon linker, data set a)

2CG0 の概要

• エントリーDOI: 10.2210/pdb2cg0/pdb
• 関連するPDBエントリー: 1AV4 1AVK 1AVL 1IQX 1IQY 1IU7 1IVU 1IVV 1IVW 1IVX 1RJO 1SIH 1SII 1UI7 1UI8 1W4N 1W5Z 1W6C 1W6G 1WMN 1WMO 1WMP 2BT3 2CFD 2CFG 2CFK 2CFL 2CFW 2CG1
• 分子名称: PHENYLETHYLAMINE OXIDASE, COPPER (II) ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: amine oxidase, arthrobacter globiformis, copper containing, oxidoreductase, tpq, cuao, quinone, ruthenium diimine wires, competitive inhibition, metal-binding
• 由来する生物種: ARTHROBACTER GLOBIFORMIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 73372.12

構造登録者

Langley, D.B.,Duff, A.P.,Freeman, H.C.,Guss, J.M.,Juda, G.A.,Dooley, D.M.,Contakes, S.M.,Halpern-Manners, N.W.,Dunn, A.R.,Gray, H.B. (登録日: 2006-02-27, 公開日: 2007-05-01, 最終更新日: 2025-04-09)

主引用文献

Langley, D.B.,Brown, D.E.,Cheruzel, L.E.,Contakes, S.M.,Duff, A.P.,Hilmer, K.M.,Dooley, D.M.,Gray, H.B.,Guss, J.M.,Freeman, H.C.
Enantiomer-Specific Binding of Ruthenium(II) Molecular Wires by the Amine Oxidase of Arthrobacter Globiformis.
J.Am.Chem.Soc., 130:8069-, 2008

PubMed Abstract: The copper amine oxidase from Arthrobacter globiformis (AGAO) is reversibly inhibited by molecular wires comprising a Ru(II) complex head group and an aromatic tail group joined by an alkane linker. The crystal structures of a series of Ru(II)-wire-AGAO complexes differing with respect to the length of the alkane linker have been determined. All wires lie in the AGAO active-site channel, with their aromatic tail group in contact with the trihydroxyphenylalanine quinone (TPQ) cofactor of the enzyme. The TPQ cofactor is consistently in its active ("off-Cu") conformation, and the side chain of the so-called "gate" residue Tyr296 is consistently in the "gate-open" conformation. Among the wires tested, the most stable complex is produced when the wire has a -(CH2)4- linker. In this complex, the Ru(II)(phen)(bpy)2 head group is level with the protein molecular surface. Crystal structures of AGAO in complex with optically pure forms of the C4 wire show that the linker and head group in the two enantiomers occupy slightly different positions in the active-site channel. Both the Lambda and Delta isomers are effective competitive inhibitors of amine oxidation. Remarkably, inhibition by the C4 wire shows a high degree of selectivity for AGAO in comparison with other copper-containing amine oxidases.

PubMed: 18507382
DOI: 10.1021/JA801289F

実験手法

X-RAY DIFFRACTION (1.8 Å)