1wmo

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[[Image:1wmo.gif|left|200px]]
[[Image:1wmo.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1wmo |SIZE=350|CAPTION= <scene name='initialview01'>1wmo</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1wmo", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1wmo| PDB=1wmo | SCENE= }}
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|RELATEDENTRY=[[1iu7|1IU7]], [[1iqx|1IQX]], [[1iqy|1IQY]], [[1wmn|1WMN]], [[1wmp|1WMP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wmo OCA], [http://www.ebi.ac.uk/pdbsum/1wmo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wmo RCSB]</span>
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}}
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'''Crystal structure of topaquinone-containing amine oxidase activated by nickel ion'''
'''Crystal structure of topaquinone-containing amine oxidase activated by nickel ion'''
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==Reference==
==Reference==
Reinvestigation of metal ion specificity for quinone cofactor biogenesis in bacterial copper amine oxidase., Okajima T, Kishishita S, Chiu YC, Murakawa T, Kim M, Yamaguchi H, Hirota S, Kuroda S, Tanizawa K, Biochemistry. 2005 Sep 13;44(36):12041-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16142901 16142901]
Reinvestigation of metal ion specificity for quinone cofactor biogenesis in bacterial copper amine oxidase., Okajima T, Kishishita S, Chiu YC, Murakawa T, Kim M, Yamaguchi H, Hirota S, Kuroda S, Tanizawa K, Biochemistry. 2005 Sep 13;44(36):12041-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16142901 16142901]
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[[Category: Amine oxidase (copper-containing)]]
 
[[Category: Arthrobacter globiformis]]
[[Category: Arthrobacter globiformis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Tanizawa, K.]]
[[Category: Tanizawa, K.]]
[[Category: Yamaguchi, H.]]
[[Category: Yamaguchi, H.]]
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[[Category: amine oxidase]]
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[[Category: Amine oxidase]]
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[[Category: biogenesis]]
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[[Category: Biogenesis]]
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[[Category: copper]]
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[[Category: Copper]]
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[[Category: nickel]]
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[[Category: Nickel]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: topaquinone]]
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[[Category: Topaquinone]]
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[[Category: tpq]]
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[[Category: Tpq]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:52:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:38:19 2008''
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Revision as of 10:52, 3 May 2008

Image:1wmo.gif

Template:STRUCTURE 1wmo

Crystal structure of topaquinone-containing amine oxidase activated by nickel ion


Overview

The topa quinone (TPQ) cofactor of copper amine oxidase is generated by copper-assisted self-processing of the precursor protein. Metal ion specificity for TPQ biogenesis has been reinvestigated with the recombinant phenylethylamine oxidase from Arthrobacter globiformis. Besides Cu2+ ion, some divalent metal ions such as Co2+, Ni2+, and Zn2+ were also bound to the metal site of the apoenzyme so tightly that they were not replaced by excess Cu2+ ions added subsequently. Although these noncupric metal ions could not initiate TPQ formation under the atmospheric conditions, we observed slow spectral changes in the enzyme bound with Co2+ or Ni2+ ion under the dioxygen-saturating conditions. Resonance Raman spectroscopy and titration with phenylhydrazine provided unambiguous evidence for TPQ formation by Co2+ and Ni2+ ions. Steady-state kinetic analysis showed that the enzymes activated by Co2+ and Ni2+ ions were indistinguishable from the corresponding metal-substituted enzymes prepared from the native copper enzyme (Kishishita, S., Okajima, T., Kim, M., Yamaguchi, H., Hirota, S., Suzuki, S., Kuroda, S., Tanizawa, K., and Mure, M. (2003) J. Am. Chem. Soc. 125, 1041-1055). X-ray crystallographic analysis has also revealed structural identity of the active sites of Co- and Ni-activated enzymes with Cu-enzyme. Thus Cu2+ ion is not the sole metal ion assisting TPQ formation. Co2+ and Ni2+ ions are also capable of forming TPQ, though much less efficiently than Cu2+.

About this Structure

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

Reference

Reinvestigation of metal ion specificity for quinone cofactor biogenesis in bacterial copper amine oxidase., Okajima T, Kishishita S, Chiu YC, Murakawa T, Kim M, Yamaguchi H, Hirota S, Kuroda S, Tanizawa K, Biochemistry. 2005 Sep 13;44(36):12041-8. PMID:16142901 Page seeded by OCA on Sat May 3 13:52:56 2008

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