3pjk: Difference between revisions
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==Urate oxidase under 1.0 MPa / 10 bars pressure of xenon== | ==Urate oxidase under 1.0 MPa / 10 bars pressure of xenon== | ||
<StructureSection load='3pjk' size='340' side='right' caption='[[3pjk]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3pjk' size='340' side='right'caption='[[3pjk]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pjk]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3pjk]] 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=3PJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PJK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.701Å</td></tr> | ||
<tr id=' | <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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=XE:XENON'>XE</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=3pjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pjk OCA], [https://pdbe.org/3pjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pjk RCSB], [https://www.ebi.ac.uk/pdbsum/3pjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pjk ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3pjk" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Urate | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Aspergillus flavus]] | [[Category: Aspergillus flavus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Abraini | [[Category: Abraini JH]] | ||
[[Category: | [[Category: Colloc'h N]] | ||
[[Category: Marassio G]] | |||
[[Category: Prange T]] | |||
[[Category: | |||
[[Category: T | |||
Latest revision as of 12:55, 6 September 2023
Urate oxidase under 1.0 MPa / 10 bars pressure of xenonUrate oxidase under 1.0 MPa / 10 bars pressure of xenon
Structural highlights
FunctionURIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. Publication Abstract from PubMedThe remarkably safe anesthetics xenon (Xe) and, to lesser extent, nitrous oxide (N(2)O) possess neuroprotective properties in preclinical studies. To investigate the mechanisms of pharmacological action of these gases, which are still poorly known, we performed both crystallography under a large range of gas pressure and biochemical studies on urate oxidase, a prototype of globular gas-binding proteins whose activity is modulated by inert gases. We show that Xe and N(2)O bind to, compete for, and expand the volume of a hydrophobic cavity located just behind the active site of urate oxidase and further inhibit urate oxidase enzymatic activity. By demonstrating a significant relationship between the binding and biochemical effects of Xe and N(2)O, given alone or in combination, these data from structure to function highlight the mechanisms by which chemically and metabolically inert gases can alter protein function and produce their pharmacological effects. Interestingly, the effects of a Xe:N(2)O equimolar mixture were found to be equivalent to those of Xe alone, thereby suggesting that gas mixtures containing Xe and N(2)O could be an alternative and efficient neuroprotective strategy to Xe alone, whose widespread clinical use is limited due to the cost of production and availability of this gas.-Marassio, G., Prange, T., David, H. N., Sopkova-de Oliveira Santos, J., Gabison, L., Delcroix, N., Abraini, J. H., Colloc'h, N. Pressure-response analysis of anesthetic gases xenon and nitrous oxide on urate oxidase: a crystallographic study. Pressure-response analysis of anesthetic gases xenon and nitrous oxide on urate oxidase: a crystallographic study.,Marassio G, Prange T, David HN, Sopkova-de Oliveira Santos J, Gabison L, Delcroix N, Abraini JH, Colloc'h N FASEB J. 2011 Mar 18. PMID:21421845[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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