3plm: Difference between revisions

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==Urate oxidase under 2.0 MPa / 20 bars pressure of equimolar mixture xenon : nitrous oxide==
==Urate oxidase under 2.0 MPa / 20 bars pressure of equimolar mixture xenon : nitrous oxide==
<StructureSection load='3plm' size='340' side='right' caption='[[3plm]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
<StructureSection load='3plm' size='340' side='right'caption='[[3plm]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3plm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PLM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PLM FirstGlance]. <br>
<table><tr><td colspan='2'>[[3plm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspfl Aspfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PLM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=N2O:NITROUS+OXIDE'>N2O</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=N2O:NITROUS+OXIDE'>N2O</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pjk|3pjk]], [[3pk3|3pk3]], [[3pk4|3pk4]], [[3pk5|3pk5]], [[3pk6|3pk6]], [[3pk8|3pk8]], [[3pkf|3pkf]], [[3pkg|3pkg]], [[3pkh|3pkh]], [[3pkk|3pkk]], [[3pkl|3pkl]], [[3pks|3pks]], [[3pkt|3pkt]], [[3pku|3pku]], [[3ple|3ple]], [[3plg|3plg]], [[3plh|3plh]], [[3pli|3pli]], [[3plj|3plj]], [[2ic0|2ic0]], [[2icq|2icq]], [[2iba|2iba]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pjk|3pjk]], [[3pk3|3pk3]], [[3pk4|3pk4]], [[3pk5|3pk5]], [[3pk6|3pk6]], [[3pk8|3pk8]], [[3pkf|3pkf]], [[3pkg|3pkg]], [[3pkh|3pkh]], [[3pkk|3pkk]], [[3pkl|3pkl]], [[3pks|3pks]], [[3pkt|3pkt]], [[3pku|3pku]], [[3ple|3ple]], [[3plg|3plg]], [[3plh|3plh]], [[3pli|3pli]], [[3plj|3plj]], [[2ic0|2ic0]], [[2icq|2icq]], [[2iba|2iba]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uaZ, uox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 ASPFL])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uaZ, uox ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 ASPFL])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Factor_independent_urate_hydroxylase Factor independent urate hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Factor_independent_urate_hydroxylase Factor independent urate hydroxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3] </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=3plm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3plm OCA], [http://pdbe.org/3plm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3plm RCSB], [http://www.ebi.ac.uk/pdbsum/3plm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3plm ProSAT]</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=3plm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3plm OCA], [https://pdbe.org/3plm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3plm RCSB], [https://www.ebi.ac.uk/pdbsum/3plm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3plm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[[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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</div>
</div>
<div class="pdbe-citations 3plm" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3plm" style="background-color:#fffaf0;"></div>
==See Also==
*[[Urate Oxidase|Urate Oxidase]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Aspfl]]
[[Category: Aspfl]]
[[Category: Factor independent urate hydroxylase]]
[[Category: Factor independent urate hydroxylase]]
[[Category: Large Structures]]
[[Category: Abraini, J H]]
[[Category: Abraini, J H]]
[[Category: Marassio, G]]
[[Category: Marassio, G]]

Revision as of 11:44, 25 May 2022

Urate oxidase under 2.0 MPa / 20 bars pressure of equimolar mixture xenon : nitrous oxideUrate oxidase under 2.0 MPa / 20 bars pressure of equimolar mixture xenon : nitrous oxide

Structural highlights

3plm is a 1 chain structure with sequence from Aspfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:
Gene:uaZ, uox (ASPFL)
Activity:Factor independent urate hydroxylase, with EC number 1.7.3.3
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[URIC_ASPFL] Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.

Publication Abstract from PubMed

The 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 Also

References

  1. Marassio G, Prange T, David HN, Sopkova-de Oliveira Santos J, Gabison L, Delcroix N, Abraini JH, Colloc'h N. Pressure-response analysis of anesthetic gases xenon and nitrous oxide on urate oxidase: a crystallographic study. FASEB J. 2011 Mar 18. PMID:21421845 doi:10.1096/fj.11-183046

3plm, resolution 1.62Å

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