View source for 2xq1


==Crystal structure of peroxisomal catalase from the yeast Hansenula polymorpha==
<StructureSection load='2xq1' size='340' side='right'caption='[[2xq1]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xq1]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Ogataea_angusta Ogataea angusta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XQ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XQ1 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]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=2xq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xq1 OCA], [https://pdbe.org/2xq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xq1 RCSB], [https://www.ebi.ac.uk/pdbsum/2xq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xq1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CATA_PICAN CATA_PICAN] Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The reactive oxygen species hydrogen peroxide is a byproduct of the beta-oxidation process that occurs in peroxisomes. Since reactive oxygen species can cause serious damage to biomolecules, a number of scavengers control their intracellular levels. One such scavenger that is present in the peroxisome is the oxidoreductase catalase. In this study, the crystal structure of heterologously expressed peroxisomal catalase from the thermotolerant yeast Hansenula polymorpha has been determined at 2.9 A resolution. H. polymorpha catalase is a typical peroxisomal catalase; it is tetrameric and is highly similar to catalases from other organisms. However, its hydrogen peroxide-degrading activity is higher than those of a number of other catalases for which structural data are available. Structural superimpositions indicate that the nature of the major channel, the path for hydrogen peroxide to the active site, varies from those seen in other catalase structures, an observation that may account for the high activity of H. polymorpha catalase.

Structural features of peroxisomal catalase from the yeast Hansenula polymorpha.,Pena-Soler E, Vega MC, Wilmanns M, Williams C Acta Crystallogr D Biol Crystallogr. 2011 Aug;67(Pt 8):690-8. Epub 2011 Jul 12. PMID:21795810<ref>PMID:21795810</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2xq1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Catalase 3D structures|Catalase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ogataea angusta]]
[[Category: Penya-Soler E]]
[[Category: Vega MC]]
[[Category: Williams CP]]
[[Category: Wilmanns M]]