4op6: Difference between revisions
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== | ==Urate OXIDASE + 8-AZAXANTHINE UNDER 40 BARS OXYGEN== | ||
[[http://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL | <StructureSection load='4op6' size='340' side='right'caption='[[4op6]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4op6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OP6 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]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=4op6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4op6 OCA], [https://pdbe.org/4op6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4op6 RCSB], [https://www.ebi.ac.uk/pdbsum/4op6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4op6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/URIC_ASPFL URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Urate oxidase from Aspergillus flavus is a 135 kDa homo-tetramer which has a hydrophobic cavity buried within each monomer and located close to its active site. Crystallographic studies under moderate gas pressure and high hydrostatic pressure have shown that both gas presence and high pressure would rigidify the cavity leading to an inhibition of the catalytic activity. Analysis of the cavity volume variations and functional modifications suggest that the flexibility of the cavity would be an essential parameter for the active site efficiency. This cavity would act as a connecting vessel to give flexibility to the neighboring active site, and its expansion under pure oxygen pressure reveals that it might serve as a transient reservoir on its pathway to the active site. | |||
Functional relevance of the internal hydrophobic cavity of urate oxidase.,Colloc'h N, Prange T FEBS Lett. 2014 May 2;588(9):1715-9. doi: 10.1016/j.febslet.2014.03.017. Epub, 2014 Mar 18. PMID:24657440<ref>PMID:24657440</ref> | |||
[[ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 4op6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
[[Category: | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: T | __TOC__ | ||
</StructureSection> | |||
[[Category: Aspergillus flavus]] | |||
[[Category: Large Structures]] | |||
[[Category: Colloc'h N]] | |||
[[Category: Prange T]] | |||
Latest revision as of 17:57, 8 November 2023
Urate OXIDASE + 8-AZAXANTHINE UNDER 40 BARS OXYGENUrate OXIDASE + 8-AZAXANTHINE UNDER 40 BARS OXYGEN
Structural highlights
FunctionURIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. Publication Abstract from PubMedUrate oxidase from Aspergillus flavus is a 135 kDa homo-tetramer which has a hydrophobic cavity buried within each monomer and located close to its active site. Crystallographic studies under moderate gas pressure and high hydrostatic pressure have shown that both gas presence and high pressure would rigidify the cavity leading to an inhibition of the catalytic activity. Analysis of the cavity volume variations and functional modifications suggest that the flexibility of the cavity would be an essential parameter for the active site efficiency. This cavity would act as a connecting vessel to give flexibility to the neighboring active site, and its expansion under pure oxygen pressure reveals that it might serve as a transient reservoir on its pathway to the active site. Functional relevance of the internal hydrophobic cavity of urate oxidase.,Colloc'h N, Prange T FEBS Lett. 2014 May 2;588(9):1715-9. doi: 10.1016/j.febslet.2014.03.017. Epub, 2014 Mar 18. PMID:24657440[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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