1ui7: Difference between revisions

Revision as of 21:43, 28 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:1ui7.png

Template:STRUCTURE 1ui7

Site-directed mutagenesis of His433 involved in binding of copper ion in Arthrobacter globiformis amine oxidaseSite-directed mutagenesis of His433 involved in binding of copper ion in Arthrobacter globiformis amine oxidase

Template:ABSTRACT PUBMED 14979714

About this StructureAbout this Structure

1UI7 is a Single protein structure of sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA.

ReferenceReference

Chemical rescue of a site-specific mutant of bacterial copper amine oxidase for generation of the topa quinone cofactor., Matsunami H, Okajima T, Hirota S, Yamaguchi H, Hori H, Kuroda S, Tanizawa K, Biochemistry. 2004 Mar 2;43(8):2178-87. PMID:14979714

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OCA

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-'''Site-directed mutagenesis of His433 involved in binding of copper ion in Arthrobacter globiformis amine oxidase'''
+===Site-directed mutagenesis of His433 involved in binding of copper ion in Arthrobacter globiformis amine oxidase===
-==Overview==
+<!--
-The topa quinone (TPQ) cofactor of copper amine oxidase is produced by posttranslational modification of a specific tyrosine residue through the copper-dependent, self-catalytic process. We have site-specifically mutated three histidine residues (His431, His433, and His592) involved in binding of the copper ion in the recombinant phenylethylamine oxidase from Arthrobacter globiformis. The mutant enzymes, in which each histidine was replaced by alanine, were purified in the Cu/TPQ-free precursor form and analyzed for their Cu-binding and TPQ-generating activities by UV-visible absorption, resonance Raman, and electron paramagnetic resonance spectroscopies. Among the three histidine-to-alanine mutants, only H592A was found to show a weak activity to form TPQ upon aerobic incubation with Cu(2+) ions. Also for H592A, exogenous imidazole rescued binding of copper and markedly promoted the TPQ formation. Accommodation of a free imidazole molecule within the cavity created in the active site of H592A was suggested by X-ray crystallography. Although the TPQ cofactor in H592A mutant was readily reduced with substrate, its catalytic activity was very low even in the presence of imidazole. Combined with the crystal structures of the mutant enzymes, these results demonstrate the importance of the three copper-binding histidine residues for both TPQ biogenesis and catalytic activity, fine-tuning the position of the essential metal.
+The line below this paragraph, {{ABSTRACT_PUBMED_14979714}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14979714 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14979714}}
 ==About this Structure==
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 [[Category: Quinone cofactor]]
 [[Category: Tpq]]
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