1IVV

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

Summary for 1IVV

• Entry DOI: 10.2210/pdb1ivv/pdb
• Related: 1AV4 1AVK 1AVL 1IQX 1IQY 1IU7 1IVU 1IVW 1IVX
• Descriptor: amine oxidase, COPPER (II) ION (3 entities in total)
• Functional Keywords: oxidoreductase, amine oxidase, biogenesis, tpq, freeze-trapp, intermediate, quinone cofactor, dah
• Biological source: Arthrobacter globiformis
• Total number of polymer chains: 2
• Total formula weight: 141604.61

Authors

Kim, M.,Okajima, T.,Kishishita, S.,Yoshimura, M.,Kawamori, A.,Tanizawa, K.,Yamaguchi, H. (deposition date: 2002-03-29, release date: 2002-08-07, Last modification date: 2024-10-30)

Primary citation

Kim, M.,Okajima, T.,Kishishita, S.,Yoshimura, M.,Kawamori, A.,Tanizawa, K.,Yamaguchi, H.
X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase.
Nat.Struct.Biol., 9:591-596, 2002

PubMed Abstract: 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.

PubMed: 12134140
DOI: 10.1038/nsb824

Experimental method

X-RAY DIFFRACTION (2.1 Å)