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1iqy

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[[Image:1iqy.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF NICKEL-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS==
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|PDB= 1iqy |SIZE=350|CAPTION= <scene name='initialview01'>1iqy</scene>, resolution 1.8&Aring;
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<StructureSection load='1iqy' size='340' side='right'caption='[[1iqy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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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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<table><tr><td colspan='2'>[[1iqy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IQY FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqy OCA], [https://pdbe.org/1iqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iqy RCSB], [https://www.ebi.ac.uk/pdbsum/1iqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iqy ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1av4|1AV4]], [[1avl|1AVL]], [[1avk|1AVK]], [[1iqx|1IQX]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqy OCA], [http://www.ebi.ac.uk/pdbsum/1iqy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iqy RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/1iqy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1iqy ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF NICKEL-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS'''
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==See Also==
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*[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The role of the active site Cu(2+) of phenylethylamine oxidase from Arthrobacter globiformis (AGAO) has been studied by substitution with other divalent cations, where we were able to remove &gt;99.5% of Cu(2+) from the active site. The enzymes reconstituted with Co(2+) and Ni(2+) (Co- and Ni-AGAO) exhibited 2.2 and 0.9% activities, respectively, of the original Cu(2+)-enzyme (Cu-AGAO), but their K(m) values for amine substrate and dioxygen were comparable. X-ray crystal structures of the Co- and Ni-AGAO were solved at 2.0-1.8 A resolution. These structures revealed changes in the metal coordination environment when compared to that of Cu-AGAO. However, the hydrogen-bonding network around the active site involving metal-coordinating and noncoordinating water molecules was preserved. Upon anaerobic mixing of the Cu-, Co-, and Ni-AGAO with amine substrate, the 480 nm absorption band characteristic of the oxidized form of the topaquinone cofactor (TPQ(ox)) disappeared rapidly (&lt; 6 ms), yielding the aminoresorcinol form of the reduced cofactor (TPQ(amr)). In contrast to the substrate-reduced Cu-AGAO, the semiquinone radical (TPQ(sq)) was not detected in Co- and Ni-AGAO. Further, in the latter, TPQ(amr) reacted reversibly with the product aldehyde to form a species with a lambda(max) at around 350 nm that was assigned as the neutral form of the product Schiff base (TPQ(pim)). Introduction of dioxygen to the substrate-reduced Co- and Ni-AGAO resulted in the formation of a TPQ-related intermediate absorbing at around 360 nm, which was assigned to the neutral iminoquinone form of the 2e(-)-oxidized cofactor (TPQ(imq)) and which decayed concomitantly with the generation of TPQ(ox). The rate of TPQ(imq) formation and its subsequent decay in Co- and Ni-AGAO was slow when compared to those of the corresponding reactions in Cu-AGAO. The low catalytic activities of the metal-substituted enzymes are due to the impaired efficiencies of the oxidative half-reaction in the catalytic cycle of amine oxidation. On the basis of these results, we propose that the native Cu(2+) ion has essential roles such as catalyzing the electron transfer between TPQ(amr) and dioxygen, in part by providing a binding site for 1e(-)- and 2e(-)-reduced dioxygen species to be efficiently protonated and released and also preventing the back reaction between the product aldehyde and TPQ(amr).
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==About this Structure==
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1IQY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQY OCA].
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==Reference==
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Role of copper ion in bacterial copper amine oxidase: spectroscopic and crystallographic studies of metal-substituted enzymes., Kishishita S, Okajima T, Kim M, Yamaguchi H, Hirota S, Suzuki S, Kuroda S, Tanizawa K, Mure M, J Am Chem Soc. 2003 Jan 29;125(4):1041-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12537504 12537504]
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[[Category: Amine oxidase (copper-containing)]]
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[[Category: Arthrobacter globiformis]]
[[Category: Arthrobacter globiformis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hirota, S.]]
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[[Category: Hirota S]]
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[[Category: Kim, M.]]
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[[Category: Kim M]]
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[[Category: Kishishita, S.]]
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[[Category: Kishishita S]]
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[[Category: Kuroda, S.]]
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[[Category: Kuroda S]]
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[[Category: Mure, M.]]
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[[Category: Mure M]]
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[[Category: Okajima, T.]]
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[[Category: Okajima T]]
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[[Category: Tanizawa, K.]]
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[[Category: Tanizawa K]]
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[[Category: Yamaguchi, H.]]
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[[Category: Yamaguchi H]]
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[[Category: amine oxidase]]
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[[Category: arthrobacter globiformi]]
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[[Category: copper]]
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[[Category: ni(ii)]]
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[[Category: nickel]]
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[[Category: oxidoreductase]]
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[[Category: quinone cofactor]]
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[[Category: tpq]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:22 2008''
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Current revision

CRYSTAL STRUCTURE OF NICKEL-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS

PDB ID 1iqy

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