1a2v

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[[Image:1a2v.gif|left|200px]]
 
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{{Structure
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==COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA==
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|PDB= 1a2v |SIZE=350|CAPTION= <scene name='initialview01'>1a2v</scene>, resolution 2.40&Aring;
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<StructureSection load='1a2v' size='340' side='right'caption='[[1a2v]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
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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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|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]
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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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|GENE=
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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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}}
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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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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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[[Category: Amine oxidase (copper-containing)]]
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[[Category: Pichia angusta]]
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[[Category: Single protein]]
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[[Category: Li, R.]]
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[[Category: Mathews, F S.]]
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[[Category: CU]]
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[[Category: amine oxidase]]
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[[Category: quinoprotein]]
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[[Category: topaquinone enzyme]]
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[[Category: tpq]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:04 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1a2v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Ogataea angusta]]
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[[Category: Li R]]
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[[Category: Mathews FS]]

Current revision

COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA

PDB ID 1a2v

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