1ivx: Difference between revisions
New page: left|200px<br /><applet load="1ivx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ivx, resolution 2.2Å" /> '''Crystal structure of ... |
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[[Image:1ivx.gif|left|200px]]<br /><applet load="1ivx" size=" | [[Image:1ivx.gif|left|200px]]<br /><applet load="1ivx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ivx, resolution 2.2Å" /> | caption="1ivx, resolution 2.2Å" /> | ||
'''Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.'''<br /> | '''Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.'''<br /> | ||
==Overview== | ==Overview== | ||
The quinone cofactor TPQ in copper amine oxidase is generated by | 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== | ||
1IVX 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:// | 1IVX 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=1IVX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tpq]] | [[Category: tpq]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:10 2008'' | ||
Revision as of 14:16, 21 February 2008
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Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.
OverviewOverview
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 StructureAbout this Structure
1IVX 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.
ReferenceReference
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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