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| | <StructureSection load='3amo' size='340' side='right'caption='[[3amo]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='3amo' size='340' side='right'caption='[[3amo]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3amo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"achromobacter_globiformis"_(conn_1928)_bergey_et_al._1930 "achromobacter globiformis" (conn 1928) bergey et al. 1930]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AMO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3amo]] 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=3AMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AMO 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1TY:3-{(3E)-4-HYDROXY-6-OXO-3-[(2-PHENYLETHYL)IMINO]CYCLOHEXA-1,4-DIEN-1-YL}ALANINE'>1TY</scene>, <scene name='pdbligand=2TY:2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE'>2TY</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1TY:3-{(3E)-4-HYDROXY-6-OXO-3-[(2-PHENYLETHYL)IMINO]CYCLOHEXA-1,4-DIEN-1-YL}ALANINE'>1TY</scene>, <scene name='pdbligand=2TY:2-HYDROXY-5-{[(1E)-2-PHENYLETHYLIDENE]AMINO}-L-TYROSINE'>2TY</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1av4|1av4]], [[2cfd|2cfd]], [[1iu7|1iu7]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Primary-amine_oxidase Primary-amine oxidase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3amo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3amo OCA], [https://pdbe.org/3amo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3amo RCSB], [https://www.ebi.ac.uk/pdbsum/3amo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3amo ProSAT]</span></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=3amo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3amo OCA], [https://pdbe.org/3amo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3amo RCSB], [https://www.ebi.ac.uk/pdbsum/3amo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3amo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAOX_ARTGO PAOX_ARTGO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Arthrobacter globiformis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Primary-amine oxidase]]
| + | [[Category: Kataoka M]] |
| - | [[Category: Kataoka, M]] | + | [[Category: Okajima T]] |
| - | [[Category: Okajima, T]] | + | [[Category: Otsu M]] |
| - | [[Category: Otsu, M]] | + | [[Category: Oya H]] |
| - | [[Category: Oya, H]] | + | [[Category: Tanizawa K]] |
| - | [[Category: Tanizawa, K]] | + | [[Category: Tominaga A]] |
| - | [[Category: Tominaga, A]] | + | [[Category: Yamaguchi H]] |
| - | [[Category: Yamaguchi, H]] | + | |
| - | [[Category: Amine oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Phenylethylamine]]
| + | |
| - | [[Category: Product schiff-base]]
| + | |
| - | [[Category: Reaction intermediate]]
| + | |
| - | [[Category: Substrate schiff-base]]
| + | |
| - | [[Category: Topaquinone]]
| + | |
| - | [[Category: Tpq]]
| + | |
| - | [[Category: Tpq biogenesis]]
| + | |
| Structural highlights
3amo is a 2 chain structure with sequence from Arthrobacter globiformis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.1Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PAOX_ARTGO
Publication Abstract from PubMed
To reveal the chemical changes and geometry changes of active-site residues that cooperate with a reaction is important for understanding the functional mechanism of proteins. Consecutive temporal analyses of enzyme structures have been performed during reactions to clarify structure-based reaction mechanisms. Phenylethylamine oxidase from Arthrobacter globiformis (AGAO) contains a copper ion and topaquinone (TPQ(ox)). The catalytic reaction of AGAO catalyzes oxidative deaminations of phenylethylamine and consists of reductive and oxidative half-reactions. In the reduction step, TPQ(ox) reacts with a phenylethylamine (PEA) substrate giving rise to a topasemiquinone (TPQ(sq)) formed Schiff-base and produces phenylacetaldehyde. To elucidate the mechanism of the reductive half-reaction, an attempt was made to trap the reaction intermediates in order to analyze their structures. The reaction proceeded within the crystals when AGAO crystals were soaked in a PEA solution and freeze-trapped in liquid nitrogen. The reaction stage of each crystal was confirmed by single-crystal microspectrometry, before X-ray diffraction measurements were made of four reaction intermediates. The structure at 15 min after the onset of the reaction was analyzed at atomic resolution, and it was shown that TPQ(ox) and some residues in the substrate channel were alternated via catalytic reductive half-reactions.
Detection of the reaction intermediates catalyzed by a copper amine oxidase.,Kataoka M, Oya H, Tominaga A, Otsu M, Okajima T, Tanizawa K, Yamaguchi H J Synchrotron Radiat. 2011 Jan;18(1):58-61. Epub 2010 Nov 5. PMID:21169693[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kataoka M, Oya H, Tominaga A, Otsu M, Okajima T, Tanizawa K, Yamaguchi H. Detection of the reaction intermediates catalyzed by a copper amine oxidase. J Synchrotron Radiat. 2011 Jan;18(1):58-61. Epub 2010 Nov 5. PMID:21169693 doi:10.1107/S0909049510034989
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