5y17: Difference between revisions
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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 [ | <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=' | </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=' | <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'>[ | <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 == | ||
[ | [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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycothermus thermophilus]] | ||
[[Category: | [[Category: Balci S]] | ||
[[Category: | [[Category: Goc G]] | ||
[[Category: Karakus Yuzugullu Y]] | |||
[[Category: Yuzugullu | [[Category: Pearson AR]] | ||
[[Category: | [[Category: Yorke B]] | ||
[[Category: | |||
Latest revision as of 11:18, 22 November 2023
CATPO mutant - E316FCATPO mutant - E316F
Structural highlights
FunctionM4GGR7_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 PubMedThe 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 AlsoReferences
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