1ivv: Difference between revisions

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[[Image:1ivv.~~jpg~~|left|200px]]

[[Image:1ivv.png|left|200px]]

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

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

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_12134140}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12134140 is the PubMed ID number.

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==About this Structure==

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[[Category: Quinone cofactor]]

[[Category: Tpq]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 20~~:28:58 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:05:30 2008''

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-[[Image:1ivv.jpg|left|200px]]
+{{Seed}}
+[[Image:1ivv.png|left|200px]]
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 {{STRUCTURE_1ivv|  PDB=1ivv  |  SCENE=  }}
-'''Crystal structure of copper amine oxidase from Arthrobacter globiformis: Early intermediate in topaquinone biogenesis'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12134140}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12134140 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12134140}}
 ==About this Structure==
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 [[Category: Quinone cofactor]]
 [[Category: Tpq]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:28:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 14:05:30 2008''