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| - | [[Image:1iqy.jpg|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURE OF NICKEL-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS== |
| - | |PDB= 1iqy |SIZE=350|CAPTION= <scene name='initialview01'>1iqy</scene>, resolution 1.8Å
| + | <StructureSection load='1iqy' size='340' side='right'caption='[[1iqy]], [[Resolution|resolution]] 1.80Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | + | <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> |
| - | |ACTIVITY= [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]
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | |GENE= | + | <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> |
| - | }}
| + | <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> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO] |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/1iqy_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </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]. |
| | + | <div style="clear:both"></div> |
| | | | |
| - | '''CRYSTAL STRUCTURE OF NICKEL-SUBSTITUTED AMINE OXIDASE FROM ARTHROBACTER GLOBIFORMIS'''
| + | ==See Also== |
| - | | + | *[[Copper amine oxidase 3D structures|Copper amine oxidase 3D structures]] |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | 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 >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 (< 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==
| + | |
| - | 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==
| + | |
| - | 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)]]
| + | |
| | [[Category: Arthrobacter globiformis]] | | [[Category: Arthrobacter globiformis]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Hirota, S.]] | + | [[Category: Hirota S]] |
| - | [[Category: Kim, M.]] | + | [[Category: Kim M]] |
| - | [[Category: Kishishita, S.]] | + | [[Category: Kishishita S]] |
| - | [[Category: Kuroda, S.]] | + | [[Category: Kuroda S]] |
| - | [[Category: Mure, M.]] | + | [[Category: Mure M]] |
| - | [[Category: Okajima, T.]] | + | [[Category: Okajima T]] |
| - | [[Category: Tanizawa, K.]] | + | [[Category: Tanizawa K]] |
| - | [[Category: Yamaguchi, H.]] | + | [[Category: Yamaguchi H]] |
| - | [[Category: NI]]
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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 Thu Mar 20 11:53:45 2008''
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