5y2p
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Bacillus sp. TB-90 Urate Oxidase Improved by Humidity Control at 86% RH.== | |
| + | <StructureSection load='5y2p' size='340' side='right' caption='[[5y2p]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5y2p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y2P 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></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='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=5y2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y2p OCA], [http://pdbe.org/5y2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y2p RCSB], [http://www.ebi.ac.uk/pdbsum/5y2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y2p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PUCL_BACSB PUCL_BACSB]] Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The optimal activity of Bacillus sp. TB-90 urate oxidase (BTUO) is 45 degrees C, but this enzyme is one of the most thermostable urate oxidases. A marked increase (>10 degrees C) in its thermal stability is induced by high concentrations (0.8-1.2 M) of sodium sulfate. Calorimetric measurements and size exclusion chromatographic analyses suggested that sulfate-induced thermal stabilization is related to the binding of a sulfate anion that repressed the dissociation of BTUO tetramers into dimers. To determine the sulfate binding site, the crystal structure was determined at 1.75 A resolution. The bound sulfate anion was found at the subunit interface of the symmetrical related subunits and formed a salt bridge with two Arg298 residues in the flexible loop that is involved in subunit assembly. Site-directed mutagenesis of Arg298 to Glu was used to extensively characterize the sulfate binding site at the subunit interface. The network of charged hydrogen bonds via the bound sulfate is suggested to contribute significantly to the thermal stabilization of both subunit dimers and the tetrameric assembly of BTUO. Knowledge of the mechanism of salt-induced stabilization will help to develop new strategies for enhancing protein thermal stabilization. | ||
| - | + | Intersubunit Salt Bridges with a Sulfate Anion Control Subunit Dissociation and Thermal Stabilization of Bacillus sp. TB-90 Urate Oxidase.,Hibi T, Hayashi Y, Fukada H, Itoh T, Nago T, Nishiya Y Biochemistry. 2014 Jun 13. PMID:24897238<ref>PMID:24897238</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5y2p" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Factor independent urate hydroxylase]] | ||
[[Category: Itoh, T]] | [[Category: Itoh, T]] | ||
| + | [[Category: Nishiya, Y]] | ||
| + | [[Category: Enzyme activation]] | ||
| + | [[Category: Flexibility]] | ||
| + | [[Category: Loop plasticity]] | ||
| + | [[Category: Oxidase]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Ph dependence]] | ||
| + | [[Category: Protein engineering]] | ||
Revision as of 21:41, 9 August 2018
Crystal Structure of Bacillus sp. TB-90 Urate Oxidase Improved by Humidity Control at 86% RH.
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