2icq: Difference between revisions

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-[[Image:2icq.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_2icq", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_2icq|  PDB=2icq  |  SCENE=  }}
-'''urate oxidase under 2.0 MPa pressure of nitrous oxide'''
+==urate oxidase under 2.0 MPa pressure of nitrous oxide==
+<StructureSection load='2icq' size='340' side='right'caption='[[2icq]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2icq]] 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=2ICQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ICQ 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]] 1.75&#8491;</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=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=N2O:NITROUS+OXIDE'>N2O</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=2icq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2icq OCA], [https://pdbe.org/2icq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2icq RCSB], [https://www.ebi.ac.uk/pdbsum/2icq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2icq 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/ic/2icq_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=2icq 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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-ICQ 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=2ICQ OCA].
+</div>
+<div class="pdbe-citations 2icq" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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]
+*[[Urate oxidase 3D structures|Urate oxidase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Aspergillus flavus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Urate oxidase]]
+[[Category: Abraini JH]]
-[[Category: Abraini, J H.]]
+[[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: Gaz-protein complex]]
-[[Category: T-fold domain]]
-[[Category: Uric acid degradation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:20:08 2008''