1ivv

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Revision as of 15:35, 20 November 2007

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spinqualitylabelsall models 1ivv, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of copper amine oxidase from Arthrobacter globiformis: Early intermediate in topaquinone biogenesis

Overview

The quinone cofactor TPQ in copper amine oxidase is generated by, posttranslational modification of an active site tyrosine residue. Using, X-ray crystallography, we have probed the copper-dependent autooxidation, process of TPQ in the enzyme from Arthrobacter globiformis. Apo enzyme, crystals were anaerobically soaked with copper; the structure determined, from this crystal provides a view of the initial state: the unmodified, tyrosine coordinated to the bound copper. Exposure of the copper-bound, crystals to oxygen led to the formation of freeze-trapped intermediates;, structural analyses indicate that these intermediates contain, dihydroxyphenylalanine quinone and trihydroxyphenylalanine. These are the, first visualized intermediates during TPQ biogenesis in copper amine, oxidase.

About this Structure

1IVV is a Single protein structure of sequence from Arthrobacter globiformis with CU as ligand. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Full crystallographic information is available from OCA.

Reference

X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase., Kim M, Okajima T, Kishishita S, Yoshimura M, Kawamori A, Tanizawa K, Yamaguchi H, Nat Struct Biol. 2002 Aug;9(8):591-6. PMID:12134140

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