1IVX
Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.
Summary for 1IVX
| Entry DOI | 10.2210/pdb1ivx/pdb |
| Related | 1AV4 1AVK 1AVL 1IQX 1IQY 1IU7 1IVU 1IVV 1IVW |
| Descriptor | amine oxidase, COPPER (II) ION (3 entities in total) |
| Functional Keywords | oxidoreductase, copper, amine oxidase, biogenesis, tpq, freeze-trapp, intermediate, quinone cofactor |
| Biological source | Arthrobacter globiformis |
| Total number of polymer chains | 2 |
| Total formula weight | 141632.58 |
| 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: 2023-12-27) |
| 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 Cited by 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: 12134140DOI: 10.1038/nsb824 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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