1ivx: Difference between revisions

Revision as of 14:05, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ivx.png

Template:STRUCTURE 1ivx

Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.

Template:ABSTRACT PUBMED 12134140

About this StructureAbout this Structure

1IVX is a Single protein structure of sequence from Arthrobacter globiformis. 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

Page seeded by OCA on Tue Jul 1 14:05:50 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.'''
+===Crystal structure of copper amine oxidase from Arthrobacter globiformis: Holo form generated by biogenesis in crystal.===
-==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.
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+{{ABSTRACT_PUBMED_12134140}}
 ==About this Structure==
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 [[Category: Quinone cofactor]]
 [[Category: Tpq]]
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