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| | ==Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid== | | ==Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid== |
| - | <StructureSection load='5oc1' size='340' side='right' caption='[[5oc1]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5oc1' size='340' side='right'caption='[[5oc1]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5oc1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Boletus_of_the_steppes Boletus of the steppes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OC1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5oc1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pleurotus_eryngii Pleurotus eryngii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OC1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aao ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5323 Boletus of the steppes])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryl-alcohol_oxidase Aryl-alcohol oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.7 1.1.3.7] </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=5oc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oc1 OCA], [https://pdbe.org/5oc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oc1 RCSB], [https://www.ebi.ac.uk/pdbsum/5oc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oc1 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5oc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oc1 OCA], [http://pdbe.org/5oc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5oc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oc1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O94219_PLEER O94219_PLEER] |
| | <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: Aryl-alcohol oxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Boletus of the steppes]]
| + | |
| - | [[Category: Carro, J]]
| + | |
| - | [[Category: Ferreira, P]]
| + | |
| - | [[Category: Martinez, A]]
| + | |
| - | [[Category: Martinez-Julvez, M]]
| + | |
| - | [[Category: Medina, M]]
| + | |
| - | [[Category: Aao]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Lignin degradation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| | [[Category: Pleurotus eryngii]] | | [[Category: Pleurotus eryngii]] |
| | + | [[Category: Carro J]] |
| | + | [[Category: Ferreira P]] |
| | + | [[Category: Martinez A]] |
| | + | [[Category: Martinez-Julvez M]] |
| | + | [[Category: Medina M]] |
| Structural highlights
Function
O94219_PLEER
Publication Abstract from PubMed
The temperature dependence of hydride transfer from the substrate to the N5 of the FAD cofactor during the reductive half-reaction of Pleurotus eryngii aryl-alcohol oxidase (AAO) is assessed here. Kinetic isotope effects on both the pre-steady state reduction of the enzyme and its steady-state kinetics, with differently deuterated substrates, suggest an environmentally-coupled quantum-mechanical tunnelling process. Moreover, those kinetic data, along with the crystallographic structure of the enzyme in complex with a substrate analogue, indicate that AAO shows a pre-organized active site that would only require the approaching of the hydride donor and acceptor for the tunnelled transfer to take place. Modification of the enzyme's active-site architecture by replacement of Tyr92, a residue establishing hydrophobic interactions with the substrate analogue in the crystal structure, in the Y92F, Y92L and Y92W variants resulted in different temperature dependence patterns that indicated a role of this residue in modulating the transfer reaction.
Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase.,Carro J, Martinez-Julvez M, Medina M, Martinez AT, Ferreira P Phys Chem Chem Phys. 2017 Oct 18. doi: 10.1039/c7cp05904c. PMID:29043303[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carro J, Martinez-Julvez M, Medina M, Martinez AT, Ferreira P. Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase. Phys Chem Chem Phys. 2017 Oct 18. doi: 10.1039/c7cp05904c. PMID:29043303 doi:http://dx.doi.org/10.1039/c7cp05904c
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