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4ysl

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Crystal structure of SdoA from Pseudomonas putida in complex with glutathione

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 ==Crystal structure of SdoA from Pseudomonas putida in complex with glutathione==
-<StructureSection load='4ysl' size='340' side='right' caption='[[4ysl]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
+<StructureSection load='4ysl' size='340' side='right'caption='[[4ysl]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ysl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YSL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ysl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_F1 Pseudomonas putida F1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YSL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4618&#8491;</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=4ysl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ysl OCA], [http://pdbe.org/4ysl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ysl RCSB], [http://www.ebi.ac.uk/pdbsum/4ysl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ysl ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</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=4ysl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ysl OCA], [https://pdbe.org/4ysl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ysl RCSB], [https://www.ebi.ac.uk/pdbsum/4ysl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ysl ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A5VWI3_PSEP1 A5VWI3_PSEP1]
-Persulfide dioxygenases (PDOs), also known as sulfur dioxygenases (SDOs), oxidize glutathione persulfide (GSSH) to sulfite and GSH. PDOs belong to the metallo-beta-lactamase superfamily and play critical roles in animals, plants and microorganisms, including sulfide detoxification. The structures of two PDOs from human and Arabidopsis thaliana have been reported; however, little is known about the substrate binding and catalytic mechanism. The crystal structures of two bacterial PDOs from Pseudomonas putida and Myxococcus xanthus were determined at 1.5 and 2.5 A resolution, respectively. The structures of both PDOs were homo-dimers, and their metal centers and beta-lactamase folds were superimposable with those of related enzymes, especially the glyoxalases II. The PDOs share similar Fe(II) coordination and a secondary coordination sphere-based hydrogen bond network that is absent in glyoxalases II, in which the corresponding residues are involved instead in coordinating a second metal ion. The crystal structure of the complex between the Pseudomonas PDO and GSH also reveals the similarity of substrate binding between it and glyoxalases II. Further analysis implicates an identical mode of substrate binding by known PDOs. Thus, the data not only reveal the differences in metal binding and coordination between the dioxygenases and the hydrolytic enzymes in the metallo-beta-lactamase superfamily, but also provide detailed information on substrate binding by PDOs.
-Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-beta-lactamase Superfamily.,Sattler SA, Wang X, Lewis KM, DeHan PJ, Park CM, Xin Y, Liu H, Xian M, Xun L, Kang C J Biol Chem. 2015 Jun 16. pii: jbc.M115.652537. PMID:26082492<ref>PMID:26082492</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4ysl" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: DeHan, P J]]
+[[Category: Large Structures]]
-[[Category: Kang, C]]
+[[Category: Pseudomonas putida F1]]
-[[Category: Sattler, S A]]
+[[Category: DeHan PJ]]
-[[Category: Wang, X]]
+[[Category: Kang C]]
-[[Category: Xun, L]]
+[[Category: Sattler SA]]
-[[Category: Ethe1]]
+[[Category: Wang X]]
-[[Category: Glutathione]]
+[[Category: Xun L]]
-[[Category: Hydrolase]]
-[[Category: Sulfur dioxygenase]]

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Crystal structure of SdoA from Pseudomonas putida in complex with glutathione

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