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| | <StructureSection load='5y17' size='340' side='right'caption='[[5y17]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5y17' size='340' side='right'caption='[[5y17]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y17]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16463 Atcc 16463]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y17 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y17]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycothermus_thermophilus Mycothermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y17 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</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]] 2.3Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HDD:CIS-HEME+D+HYDROXYCHLORIN+GAMMA-SPIROLACTONE'>HDD</scene></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=5y17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y17 OCA], [http://pdbe.org/5y17 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y17 RCSB], [http://www.ebi.ac.uk/pdbsum/5y17 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y17 ProSAT]</span></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=5y17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y17 OCA], [https://pdbe.org/5y17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y17 RCSB], [https://www.ebi.ac.uk/pdbsum/5y17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y17 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/M4GGR7_9PEZI M4GGR7_9PEZI]] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.[RuleBase:RU004142] Serves to protect cells from the toxic effects of hydrogen peroxide.[PIRNR:PIRNR038927] | + | [https://www.uniprot.org/uniprot/M4GGR7_9PEZI M4GGR7_9PEZI] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.[RuleBase:RU004142] Serves to protect cells from the toxic effects of hydrogen peroxide.[PIRNR:PIRNR038927] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 16463]] | |
| - | [[Category: Catalase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Balci, S]] | + | [[Category: Mycothermus thermophilus]] |
| - | [[Category: Goc, G]] | + | [[Category: Balci S]] |
| - | [[Category: Pearson, A R]] | + | [[Category: Goc G]] |
| - | [[Category: Yorke, B]]
| + | [[Category: Karakus Yuzugullu Y]] |
| - | [[Category: Yuzugullu, Y Karakus]] | + | [[Category: Pearson AR]] |
| - | [[Category: Lateral channel]] | + | [[Category: Yorke B]] |
| - | [[Category: Mutant]] | + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Phenol oxidase]]
| + | |
| Structural highlights
Function
M4GGR7_9PEZI Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.[RuleBase:RU004142] Serves to protect cells from the toxic effects of hydrogen peroxide.[PIRNR:PIRNR038927]
Publication Abstract from PubMed
The catalase from Scytalidium thermophilum is a homotetramer containing a heme d in each active site. Although the enzyme has a classical monofunctional catalase fold, it also possesses oxidase activity towards a number of small organics, including catechol and phenol. In order to further investigate this, the crystal structure of the complex of the catalase with the classical catalase inhibitor 3-amino-1,2,4-triazole (3TR) was determined at 1.95 A resolution. Surprisingly, no binding to the heme site was observed; instead, 3TR occupies a binding site corresponding to the NADPH-binding pocket in mammalian catalases at the entrance to a lateral channel leading to the heme. Kinetic analysis of site-directed mutants supports the assignment of this pocket as the binding site for oxidase substrates.
Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase.,Yuzugullu Karakus Y, Goc G, Balci S, Yorke BA, Trinh CH, McPherson MJ, Pearson AR Acta Crystallogr D Struct Biol. 2018 Oct 1;74(Pt 10):979-985. doi:, 10.1107/S2059798318010628. Epub 2018 Oct 2. PMID:30289408[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yuzugullu Karakus Y, Goc G, Balci S, Yorke BA, Trinh CH, McPherson MJ, Pearson AR. Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase. Acta Crystallogr D Struct Biol. 2018 Oct 1;74(Pt 10):979-985. doi:, 10.1107/S2059798318010628. Epub 2018 Oct 2. PMID:30289408 doi:http://dx.doi.org/10.1107/S2059798318010628
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