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1ivw

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(New page: 200px<br /><applet load="1ivw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ivw, resolution 1.8&Aring;" /> '''Crystal structure of ...)
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[[Image:1ivw.gif|left|200px]]<br /><applet load="1ivw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ivw.gif|left|200px]]<br /><applet load="1ivw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ivw, resolution 1.8&Aring;" />
caption="1ivw, resolution 1.8&Aring;" />
'''Crystal structure of copper amine oxidase from Arthrobacter globiformis: Late intermediate in topaquinone biogenesis'''<br />
'''Crystal structure of copper amine oxidase from Arthrobacter globiformis: Late intermediate in topaquinone biogenesis'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1IVW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IVW OCA].
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1IVW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVW OCA].
==Reference==
==Reference==
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[[Category: tpq]]
[[Category: tpq]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:42:46 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:21 2008''

Revision as of 11:16, 21 February 2008

Image:1ivw.gif

1ivw, resolution 1.8Å

Drag the structure with the mouse to rotate

Crystal structure of copper amine oxidase from Arthrobacter globiformis: Late 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

1IVW 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

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