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| | <StructureSection load='3nbj' size='340' side='right'caption='[[3nbj]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3nbj' size='340' side='right'caption='[[3nbj]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3nbj]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NBJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3NBJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3nbj]] 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=3NBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NBJ FirstGlance]. <br> |
| - | </td></tr><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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ME0:HYDROXY-L-METHIONINE'>ME0</scene>, <scene name='pdbligand=TY8:2,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY8</scene>, <scene name='pdbligand=TY9:3,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY9</scene></td></tr> | + | <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=ME0:HYDROXY-L-METHIONINE'>ME0</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TY8:2,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY8</scene>, <scene name='pdbligand=TY9:3,4-BIS(HYDROPEROXY)-5-HYDROXY-L-PHENYLALANINE'>TY9</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a2v|1a2v]]</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=3nbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbj OCA], [https://pdbe.org/3nbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nbj RCSB], [https://www.ebi.ac.uk/pdbsum/3nbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbj ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Primary-amine_oxidase Primary-amine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.21 1.4.3.21] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3nbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nbj OCA], [http://pdbe.org/3nbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nbj RCSB], [http://www.ebi.ac.uk/pdbsum/3nbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nbj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AMO_PICAN AMO_PICAN] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Primary-amine oxidase]] | + | [[Category: Ogataea angusta]] |
| - | [[Category: Chen, Z]] | + | [[Category: Chen Z]] |
| - | [[Category: Datta, S]] | + | [[Category: Datta S]] |
| - | [[Category: DuBois, J L]] | + | [[Category: DuBois JL]] |
| - | [[Category: Klinman, J P]] | + | [[Category: Klinman JP]] |
| - | [[Category: Mathews, F S]] | + | [[Category: Mathews FS]] |
| - | [[Category: Amine oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Quinoprotein]]
| + | |
| Structural highlights
3nbj is a 6 chain structure with sequence from Ogataea angusta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.9Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
AMO_PICAN
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The copper amine oxidases carry out two copper-dependent processes: production of their own redox-active cofactor (2,4,5-trihydroxyphenylalanine quinone, TPQ) and the subsequent oxidative deamination of substrate amines. Because the same active site pocket must facilitate both reactions, individual active site residues may serve multiple roles. We have examined the roles of a strictly conserved active site tyrosine Y305 in the copper amine oxidase from Hansenula polymorpha kinetically, spetroscopically (Dubois and Klinman (2006) Biochemistry 45, 3178), and, in the present work, structurally. While the Y305A enzyme is almost identical to the wild type, a novel, highly oxygenated species replaces TPQ in the Y305F active sites. This new structure not only provides the first direct detection of peroxy intermediates in cofactor biogenesis but also indicates the critical control of oxidation chemistry that can be conferred by a single active site residue.
Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.,Chen ZW, Datta S, Dubois JL, Klinman JP, Mathews FS Biochemistry. 2010 Aug 31;49(34):7393-402. PMID:20684524[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen ZW, Datta S, Dubois JL, Klinman JP, Mathews FS. Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity. Biochemistry. 2010 Aug 31;49(34):7393-402. PMID:20684524 doi:10.1021/bi100643y
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