2CFG

AGAO in complex with wc4d3 (Ru-wire inhibitor, 4-carbon linker, delta enantiomer, data set 3)

Summary for 2CFG

• Entry DOI: 10.2210/pdb2cfg/pdb
• Related: 1AV4 1AVK 1AVL 1IQX 1IQY 1IU7 1IVU 1IVV 1IVW 1IVX 1RJO 1SIH 1SII 1UI7 1UI8 1W4N 1W5Z 1W6C 1W6G 1WMN 1WMO 1WMP 2BT3 2CFD 2CFK 2CFL
• Descriptor: PHENYLETHYLAMINE OXIDASE, COPPER (II) ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: amine oxidase, arthrobacter globiformis, copper, copper containing, oxidoreductase, tpq, quinone, ruthenium diimine wires, competitive inhibition, metal-binding
• Biological source: ARTHROBACTER GLOBIFORMIS
• Total number of polymer chains: 2
• Total formula weight: 146515.91

Authors

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. (deposition date: 2006-02-21, release date: 2007-05-01, Last modification date: 2019-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)