5oc1: Difference between revisions
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==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5oc1]] is a 1 chain structure. 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> | |||
</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> | |||
<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'>[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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:29043303</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5oc1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aryl-alcohol oxidase]] | |||
[[Category: Carro, J]] | |||
[[Category: Ferreira, P]] | |||
[[Category: Martinez, A]] | [[Category: Martinez, A]] | ||
[[Category: Martinez-Julvez, M]] | |||
[[Category: Medina, M]] | [[Category: Medina, M]] | ||
[[Category: | [[Category: Aao]] | ||
[[Category: | [[Category: Flavoprotein]] | ||
[[Category: | [[Category: Lignin degradation]] | ||
[[Category: Oxidoreductase]] | |||
[[Category: Pleurotus eryngii]] | |||
