1a2v

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[[Image:1a2v.gif|left|200px]]
 
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==COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA==
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The line below this paragraph, containing "STRUCTURE_1a2v", creates the "Structure Box" on the page.
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<StructureSection load='1a2v' size='340' side='right'caption='[[1a2v]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1a2v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Ogataea_angusta Ogataea angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A2V FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene></td></tr>
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{{STRUCTURE_1a2v| PDB=1a2v | SCENE= }}
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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=1a2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2v OCA], [https://pdbe.org/1a2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a2v RCSB], [https://www.ebi.ac.uk/pdbsum/1a2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a2v ProSAT]</span></td></tr>
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</table>
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'''COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA'''
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== Function ==
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[https://www.uniprot.org/uniprot/AMO_PICAN AMO_PICAN]
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== Evolutionary Conservation ==
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==Overview==
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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/a2/1a2v_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=1a2v ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The copper-containing amine oxidase from the yeast Hansenula polymorpha (YAO) has been crystallized and partially solved by molecular replacement. It catalyzes the oxidative deamination of primary amines by molecular oxygen to the corresponding aldehydes, ammonia and hydrogen peroxide. It contains a covalently bound redox cofactor, topa quinone, generated by post-translational modification of a single tyrosine side chain. The crystals of YAO are orthorhombic, with space-group symmetry P2(1)2(1)2(1) and unit-cell dimensions a = 138.8, b = 148.2, c = 234.0 A and diffract X-rays beyond 2.0 A resolution. Solution by molecular replacement using the E. coli amine oxidase structure [Parsons, Convery, Wilmot, Yadav, Blakeley, Corner, Philips, McPherson &amp; Knowles (1995). Structure, 3, 1171-1184] as a search model reveals that there are three dimers in the asymmetric unit in a trigonal arrangement having 32 point-group symmetry. The solution agrees well with the self-rotation function of YAO. The non-crystallographic threefold axis lies parallel to a crystallographic twofold screw axis and each dimer has twofold symmetry. Phases from the refined model based on the molecular-replacement solution were used to solve one heavy-atom derivative. Model building from the unbiased isomorphous replacement phases is in progress.
The copper-containing amine oxidase from the yeast Hansenula polymorpha (YAO) has been crystallized and partially solved by molecular replacement. It catalyzes the oxidative deamination of primary amines by molecular oxygen to the corresponding aldehydes, ammonia and hydrogen peroxide. It contains a covalently bound redox cofactor, topa quinone, generated by post-translational modification of a single tyrosine side chain. The crystals of YAO are orthorhombic, with space-group symmetry P2(1)2(1)2(1) and unit-cell dimensions a = 138.8, b = 148.2, c = 234.0 A and diffract X-rays beyond 2.0 A resolution. Solution by molecular replacement using the E. coli amine oxidase structure [Parsons, Convery, Wilmot, Yadav, Blakeley, Corner, Philips, McPherson &amp; Knowles (1995). Structure, 3, 1171-1184] as a search model reveals that there are three dimers in the asymmetric unit in a trigonal arrangement having 32 point-group symmetry. The solution agrees well with the self-rotation function of YAO. The non-crystallographic threefold axis lies parallel to a crystallographic twofold screw axis and each dimer has twofold symmetry. Phases from the refined model based on the molecular-replacement solution were used to solve one heavy-atom derivative. Model building from the unbiased isomorphous replacement phases is in progress.
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==About this Structure==
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Crystallographic study of yeast copper amine oxidase.,Li R, Chen L, Cai D, Klinman JP, Mathews FS Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):364-70. PMID:15299901<ref>PMID:15299901</ref>
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1A2V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pichia_angusta Pichia angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2V OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystallographic study of yeast copper amine oxidase., Li R, Chen L, Cai D, Klinman JP, Mathews FS, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):364-70. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299901 15299901]
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</div>
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[[Category: Pichia angusta]]
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<div class="pdbe-citations 1a2v" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Li, R.]]
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<references/>
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[[Category: Mathews, F S.]]
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__TOC__
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[[Category: Amine oxidase]]
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</StructureSection>
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[[Category: Quinoprotein]]
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[[Category: Large Structures]]
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[[Category: Topaquinone enzyme]]
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[[Category: Ogataea angusta]]
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[[Category: Tpq]]
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[[Category: Li R]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:43:39 2008''
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[[Category: Mathews FS]]

Current revision

COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA

PDB ID 1a2v

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