View source for 5xy4


==CATPO mutant - V536W==
<StructureSection load='5xy4' size='340' side='right'caption='[[5xy4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xy4]] 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=5XY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XY4 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]] 1.8&#8491;</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>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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=5xy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xy4 OCA], [https://pdbe.org/5xy4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xy4 RCSB], [https://www.ebi.ac.uk/pdbsum/5xy4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xy4 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xy4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Catalase 3D structures|Catalase 3D structures]]
== 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]]