1ivv
From Proteopedia
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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 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
Page seeded by OCA on Thu Feb 21 13:16:10 2008
Categories: Amine oxidase (copper-containing) | Arthrobacter globiformis | Single protein | Kawamori, A. | Kim, M. | Kishishita, S. | Okajima, T. | Tanizawa, K. | Yamaguchi, H. | Yoshimura, M. | CU | Amine oxidase | Biogenesis | Copper | Dah | Freeze-trapp | Intermediate | Oxidoreductase | Quinone cofactor | Tpq
