2BT3

AGAO in complex with Ruthenium-C4-wire at 1.73 angstroms

Summary for 2BT3

• Entry DOI: 10.2210/pdb2bt3/pdb
• Related: 1AV4 1AVK 1AVL 1IQX 1IQY 1IU7 1IVU 1IVV 1IVW 1IVX 1RJO 1SIH 1SII 1UI7 1UI8 1W4N 1W5Z 1W6C 1W6G
• Descriptor: PHENYLETHYLAMINE OXIDASE, COPPER (II) ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: amine oxidase, arthrobacter globiformis, copper containing, oxidoreductase, tpq, quinone, ruthenium diimine wires, competitive inhibition
• Biological source: ARTHROBACTER GLOBIFORMIS
• Total number of polymer chains: 1
• Total formula weight: 73496.13

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: 2005-05-26, release date: 2005-09-05, Last modification date: 2023-12-13)

Primary citation

Contakes, S.M.,Juda, G.A.,Langley, D.B.,Halpern-Manners, N.W.,Duff, A.P.,Dunn, A.R.,Gray, H.B.,Dooley, D.M.,Guss, J.M.,Freeman, H.C.
Reversible Inhibition of Copper Amine Oxidase Activity by Channel-Blocking Ruthenium(II) and Rhenium(I) Molecular Wires.
Proc.Natl.Acad.Sci.USA, 102:13451-, 2005

PubMed Abstract: Molecular wires comprising a Ru(II)- or Re(I)-complex head group, an aromatic tail group, and an alkane linker reversibly inhibit the activity of the copper amine oxidase from Arthrobacter globiformis (AGAO), with K(i) values between 6 muM and 37 nM. In the crystal structure of a Ru(II)-wire:AGAO conjugate, the wire occupies the AGAO active-site substrate access channel, the trihydroxyphenylalanine quinone cofactor is ordered in the "off-Cu" position with its reactive carbonyl oriented toward the inhibitor, and the "gate" residue, Tyr-296, is in the "open" position. Head groups, tail-group substituents, and linker lengths all influence wire-binding interactions with the enzyme.

PubMed: 16157884
DOI: 10.1073/PNAS.0506336102

Experimental method

X-RAY DIFFRACTION (1.73 Å)