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| - | [[Image:2iba.jpg|left|200px]] | |
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| - | {{Structure
| + | ==Urate oxidase from Aspergillus flavus complexed with its inhibitor 8-azaxanthine== |
| - | |PDB= 2iba |SIZE=350|CAPTION= <scene name='initialview01'>2iba</scene>, resolution 1.500Å
| + | <StructureSection load='2iba' size='340' side='right'caption='[[2iba]], [[Resolution|resolution]] 1.50Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>
| + | <table><tr><td colspan='2'>[[2iba]] 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=2IBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IBA FirstGlance]. <br> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Urate_oxidase Urate oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.3.3 1.7.3.3]
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | |GENE= uaZ, uox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5059 Aspergillus flavus]) | + | <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></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=2iba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iba OCA], [https://pdbe.org/2iba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iba RCSB], [https://www.ebi.ac.uk/pdbsum/2iba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iba 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. |
| | + | == Evolutionary Conservation == |
| | + | [[Image:Consurf_key_small.gif|200px|right]] |
| | + | Check<jmol> |
| | + | <jmolCheckbox> |
| | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ib/2iba_consurf.spt"</scriptWhenChecked> |
| | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | + | <text>to colour the structure by Evolutionary Conservation</text> |
| | + | </jmolCheckbox> |
| | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2iba ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia. |
| | | | |
| - | '''Urate oxidase from Aspergillus flavus complexed with its inhibitor 8-azaxanthine''' | + | Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action.,Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:17028130<ref>PMID:17028130</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 2iba" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia.
| + | *[[Urate oxidase 3D structures|Urate oxidase 3D structures]] |
| - | | + | == References == |
| - | ==About this Structure== | + | <references/> |
| - | 2IBA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_flavus Aspergillus flavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IBA OCA].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==Reference==
| + | |
| - | Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action., Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH, Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17028130 17028130]
| + | |
| | [[Category: Aspergillus flavus]] | | [[Category: Aspergillus flavus]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Urate oxidase]] | + | [[Category: Colloc'h N]] |
| - | [[Category: Prange, T.]] | + | [[Category: Prange T]] |
| - | [[Category: Retailleau, P.]] | + | [[Category: Retailleau P]] |
| - | [[Category: Santos, J Sopkova-de Oliveira.]] | + | [[Category: Sopkova-de Oliveira Santos J]] |
| - | [[Category: h, N Colloc.]]
| + | |
| - | [[Category: ACE]]
| + | |
| - | [[Category: AZA]]
| + | |
| - | [[Category: NA]]
| + | |
| - | [[Category: t-fold domain]]
| + | |
| - | [[Category: tetrameric enzyme]]
| + | |
| - | [[Category: uric acid degradation]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:26 2008''
| + | |
| Structural highlights
Function
URIC_ASPFL Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In contrast with most inhalational anesthetics, the anesthetic gases xenon (Xe) and nitrous oxide (N(2)O) act by blocking the N-methyl-d-aspartate (NMDA) receptor. Using x-ray crystallography, we examined the binding characteristics of these two gases on two soluble proteins as structural models: urate oxidase, which is a prototype of a variety of intracellular globular proteins, and annexin V, which has structural and functional characteristics that allow it to be considered as a prototype for the NMDA receptor. The structure of these proteins complexed with Xe and N(2)O were determined. One N(2)O molecule or one Xe atom binds to the same main site in both proteins. A second subsite is observed for N(2)O in each case. The gas-binding sites are always hydrophobic flexible cavities buried within the monomer. Comparison of the effects of Xe and N(2)O on urate oxidase and annexin V reveals an interesting relationship with the in vivo pharmacological effects of these gases, the ratio of the gas-binding sites' volume expansion and the ratio of the narcotic potency being similar. Given these data, we propose that alterations of cytosolic globular protein functions by general anesthetics would be responsible for the early stages of anesthesia such as amnesia and hypnosis and that additional alterations of ion-channel membrane receptor functions are required for deeper effects that progress to "surgical" anesthesia.
Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action.,Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:17028130[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Colloc'h N, Sopkova-de Oliveira Santos J, Retailleau P, Vivares D, Bonnete F, Langlois d'Estainto B, Gallois B, Brisson A, Risso JJ, Lemaire M, Prange T, Abraini JH. Protein crystallography under xenon and nitrous oxide pressure: comparison with in vivo pharmacology studies and implications for the mechanism of inhaled anesthetic action. Biophys J. 2007 Jan 1;92(1):217-24. Epub 2006 Oct 6. PMID:17028130 doi:http://dx.doi.org/10.1529/biophysj.106.093807
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