View source for 5whs


==Crystal structure of the catalase-peroxidase from Neurospora crassa at 2.6 A==
<StructureSection load='5whs' size='340' side='right'caption='[[5whs]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5whs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neurospora_crassa_OR74A Neurospora crassa OR74A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WHS 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]] 2.6&#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>, <scene name='pdbligand=TOX:1-HYDROPEROXY-L-TRYPTOPHAN'>TOX</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=5whs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5whs OCA], [https://pdbe.org/5whs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5whs RCSB], [https://www.ebi.ac.uk/pdbsum/5whs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5whs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KATG_NEUCR KATG_NEUCR] Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
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== Publication Abstract from PubMed ==
CAT-2, a cytosolic catalase-peroxidase (CP) from Neurospora crassa, which is induced during asexual spore formation, was heterologously expressed and characterized. CAT-2 had the Met-Tyr-Trp (M-Y-W) adduct required for catalase activity. Its KM for H2O2 was micromolar for peroxidase and millimolar for catalase activity. A Em = -158 mV reduction potential value was obtained and the Soret band shift suggested a mixture of low and high spin ferric iron. CAT-2 EPR spectrum at 10 K indicated an axial and a rhombic component. With peroxyacetic acid (PAA), formation of Compound I* was observed with EPR. CAT-2 homodimer crystallographic structure contained two K(+) ions; Glu107 residues were displaced to bind them. CAT-2 showed the essential amino acid residues for activity in similar positions to other CPs. CAT-2 Arg426 is oriented towards the M-Y-W adduct, interacting with the deprotonated Tyr238 hydroxyl group. A perhydroxy modification of the indole nitrogen of Trp90 was oriented toward the catalytic His91. In contrast to cytochrome c peroxidase and ascorbate peroxidase, the catalase-peroxidase heme propionates are not exposed to the solvent. Together with other N. crassa enzymes that utilize H2O2 as a substrate, CAT-2 has many tryptophan and proline residues at its surface, probably related to H2O2 selection in water.

Structure, kinetics, molecular and redox properties of a cytosolic and developmentally regulated fungal catalase-peroxidase.,Vega-Garcia V, Diaz-Vilchis A, Saucedo-Vazquez JP, Solano-Peralta A, Rudino-Pinera E, Hansberg W Arch Biochem Biophys. 2018 Jan 2;640:17-26. doi: 10.1016/j.abb.2017.12.021. PMID:29305053<ref>PMID:29305053</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5whs" style="background-color:#fffaf0;"></div>

==See Also==
*[[Catalase 3D structures|Catalase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neurospora crassa OR74A]]
[[Category: Diaz-Vilchis A]]
[[Category: Hansberg W]]
[[Category: Rudino-Pinera E]]
[[Category: Vega-Garcia V]]