5oc1: Difference between revisions
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New page: '''Unreleased structure''' The entry 5oc1 is ON HOLD until Paper Publication Authors: Carro, J., Martinez-Julvez, M., Medina, M., Martinez, A., Ferreira, P. Description: Crystal struct... |
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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 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='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='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='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> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O94219_PLEER O94219_PLEER] | |||
<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> | ||
[[Category: | <div class="pdbe-citations 5oc1" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: Martinez-Julvez | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pleurotus eryngii]] | |||
[[Category: Carro J]] | |||
[[Category: Ferreira P]] | |||
[[Category: Martinez A]] | |||
[[Category: Martinez-Julvez M]] | |||
[[Category: Medina M]] | |||
Latest revision as of 09:39, 6 December 2023
Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid
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