3wlv
From Proteopedia
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| - | ''' | + | ==Thermostable urate oxidase from Bacillus sp. TB-90== |
| + | <StructureSection load='3wlv' size='340' side='right' caption='[[3wlv]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wlv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WLV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WLV FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZA:8-AZAXANTHINE'>AZA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j2g|1j2g]]</td></tr> | ||
| + | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wlv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wlv RCSB], [http://www.ebi.ac.uk/pdbsum/3wlv PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <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> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Factor independent urate hydroxylase]] | ||
| + | [[Category: Hayashi, Y.]] | ||
| + | [[Category: Hibi, T.]] | ||
| + | [[Category: Itoh, T.]] | ||
| + | [[Category: Oxidase]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Tunnel fold motif]] | ||
Revision as of 07:48, 18 June 2014
Thermostable urate oxidase from Bacillus sp. TB-90
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