7cqy
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Tetrathionate hydrolase from Acidithiobacillus ferrooxidans mutant - D325N== | |
| + | <StructureSection load='7cqy' size='340' side='right'caption='[[7cqy]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7cqy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidithiobacillus_ferrooxidans Acidithiobacillus ferrooxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CQY 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]] 2.8003578Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7cqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cqy OCA], [https://pdbe.org/7cqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cqy RCSB], [https://www.ebi.ac.uk/pdbsum/7cqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cqy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TTH_ACIF2 TTH_ACIF2] Catalyzes the hydrolysis of tetrathionate to generate elemental sulfur, thiosulfate and sulfate.<ref>PMID:17904676</ref> <ref>PMID:25144400</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Tetrathionate hydrolase (4THase) plays an important role in dissimilatory sulfur oxidation in the acidophilic iron- and sulfur-oxidizing bacterium Acidithiobacillus ferrooxidans. The structure of recombinant 4THase from A. ferrooxidans (Af-Tth) was determined by X-ray crystallography to a resolution of 1.95 A. Af-Tth is a homodimer, and its monomer structure exhibits an eight-bladed beta-propeller motif. Two insertion loops participate in dimerization, and one loop forms a cavity with the beta-propeller region. We observed unexplained electron densities in this cavity of the substrate-soaked structure. The anomalous difference map generated using diffraction data collected at a wavelength of 1.9 A indicated the presence of polymerized sulfur atoms. Asp325, a highly conserved residue among 4THases, was located near the polymerized sulfur atoms. 4THase activity was completely abolished in the site-specific Af-Tth D325N variant, suggesting that Asp325 plays a crucial role in the first step of tetrathionate hydrolysis. Considering that the Af-Tth reaction occurs only under acidic pH, Asp325 acts as an acid for the tetrathionate hydrolysis reaction. The polymerized sulfur atoms in the active site cavity may represent the intermediate product in the subsequent step. | ||
| - | + | Reaction mechanism of tetrathionate hydrolysis based on the crystal structure of tetrathionate hydrolase from Acidithiobacillus ferrooxidans.,Kanao T, Hase N, Nakayama H, Yoshida K, Nishiura K, Kosaka M, Kamimura K, Hirano Y, Tamada T Protein Sci. 2020 Oct 25. doi: 10.1002/pro.3984. PMID:33103311<ref>PMID:33103311</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Hirano | + | <div class="pdbe-citations 7cqy" style="background-color:#fffaf0;"></div> |
| - | [[Category: Tamada | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acidithiobacillus ferrooxidans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Hirano Y]] | ||
| + | [[Category: Tamada T]] | ||
Current revision
Tetrathionate hydrolase from Acidithiobacillus ferrooxidans mutant - D325N
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