2bt3 | pdb_00002bt3

AGAO IN COMPLEX WITH RUTHENIUM-C4-WIRE AT 1.73 ANGSTROMS

File:2bt3.gif

spinqualitylabelsall models 2bt3, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

Overview

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.

About this Structure

2BT3 is a [Single protein] structure of sequence from [Arthrobacter globiformis] with CU, NA, SO4, R4A and GOL as [ligands]. Active as [[1]], with EC number [1.4.3.6]. Full crystallographic information is available from [OCA].

Reference

Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires., Contakes SM, Juda GA, Langley DB, Halpern-Manners NW, Duff AP, Dunn AR, Gray HB, Dooley DM, Guss JM, Freeman HC, Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13451-6. Epub 2005 Sep 12. PMID:16157884

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