2o74: Difference between revisions

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-[[Image:2o74.gif|left|200px]]
-<!--
+==Structure of OHCU decarboxylase in complex with guanine==
-The line below this paragraph, containing "STRUCTURE_2o74", creates the "Structure Box" on the page.
+<StructureSection load='2o74' size='340' side='right'caption='[[2o74]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2o74]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O74 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GUN:GUANINE'>GUN</scene></td></tr>
-{{STRUCTURE_2o74|  PDB=2o74  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o74 OCA], [https://pdbe.org/2o74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o74 RCSB], [https://www.ebi.ac.uk/pdbsum/2o74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o74 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/URAD_DANRE URAD_DANRE] Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (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/o7/2o74_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2o74 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The complete degradation of uric acid to (S)-allantoin, as recently elucidated, involves three enzymatic reactions. Inactivation by pseudogenization of the genes of the pathway occurred during hominoid evolution, resulting in a high concentration of urate in the blood and susceptibility to gout. Here, we describe the 1.8A resolution crystal structure of the homodimeric 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase, which catalyzes the last step in the urate degradation pathway, for both ligand-free enzyme and enzyme in complex with the substrate analogs (R)-allantoin and guanine. Each monomer comprises ten alpha-helices, grouped into two domains and assembled in a novel fold. The structure and the mutational analysis of the active site have allowed us to identify some residues that are essential for catalysis, among which His-67 and Glu-87 appear to play a particularly significant role. Glu-87 may facilitate the exit of the carboxylate group because of electrostatic repulsion that destabilizes the ground state of the substrate, whereas His-67 is likely to be involved in a protonation step leading to the stereoselective formation of the (S)-allantoin enantiomer as reaction product. The structural and functional characterization of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase can provide useful information in view of the potential use of this enzyme in the enzymatic therapy of gout.
-'''Structure of OHCU decarboxylase in complex with guanine'''
+The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation.,Cendron L, Berni R, Folli C, Ramazzina I, Percudani R, Zanotti G J Biol Chem. 2007 Jun 22;282(25):18182-9. Epub 2007 Apr 11. PMID:17428786<ref>PMID:17428786</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-==About this Structure==
+</div>
-O74 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O74 OCA].
+<div class="pdbe-citations 2o74" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Danio rerio]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Berni, R.]]
+[[Category: Berni R]]
-[[Category: Cendron, L.]]
+[[Category: Cendron L]]
-[[Category: Folli, C.]]
+[[Category: Folli C]]
-[[Category: Percudani, R.]]
+[[Category: Percudani R]]
-[[Category: Ramazzina, I.]]
+[[Category: Ramazzina I]]
-[[Category: Zanotti, G.]]
+[[Category: Zanotti G]]
-[[Category: 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline]]
-[[Category: 5-hydroxyisourate]]
-[[Category: Decarboxylation]]
-[[Category: Hiu]]
-[[Category: Ohcu]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:24:29 2008''