5xvz: Difference between revisions
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==CATPO mutant - H246W== | |||
<StructureSection load='5xvz' size='340' side='right'caption='[[5xvz]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5xvz]] 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=5XVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XVZ 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]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=5xvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xvz OCA], [https://pdbe.org/5xvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xvz RCSB], [https://www.ebi.ac.uk/pdbsum/5xvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xvz ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/M4GGR7_HUMIN M4GGR7_HUMIN] Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide.[RuleBase:RU004142] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.[ARBA:ARBA00003918][PIRNR:PIRNR038927] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:30289408</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5xvz" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Pearson | *[[Catalase 3D structures|Catalase 3D structures]] | ||
[[Category: Yuzugullu Karakus | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycothermus thermophilus]] | |||
[[Category: Balci S]] | |||
[[Category: Goc G]] | |||
[[Category: Pearson AR]] | |||
[[Category: Yorke B]] | |||
[[Category: Yuzugullu Karakus Y]] | |||
