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| | <StructureSection load='3hb6' size='340' side='right'caption='[[3hb6]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3hb6' size='340' side='right'caption='[[3hb6]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hb6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29906 Atcc 29906]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HB6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hb6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HB6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m85|1m85]], [[1mqf|1mqf]], [[1nm0|1nm0]], [[2cag|2cag]], [[2cah|2cah]], [[1e93|1e93]], [[1h6n|1h6n]], [[1h7k|1h7k]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">katA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=584 ATCC 29906])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Catalase Catalase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] </span></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=3hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hb6 OCA], [https://pdbe.org/3hb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hb6 RCSB], [https://www.ebi.ac.uk/pdbsum/3hb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hb6 ProSAT]</span></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=3hb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hb6 OCA], [https://pdbe.org/3hb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hb6 RCSB], [https://www.ebi.ac.uk/pdbsum/3hb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hb6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CATA_PROMI CATA_PROMI]] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
| + | [https://www.uniprot.org/uniprot/CATA_PROMI CATA_PROMI] Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 29906]] | |
| - | [[Category: Catalase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andeoletti, P]] | + | [[Category: Proteus mirabilis]] |
| - | [[Category: Gouet, P]] | + | [[Category: Andeoletti P]] |
| - | [[Category: Jouve, H M]] | + | [[Category: Gouet P]] |
| - | [[Category: Beta-barrel]] | + | [[Category: Jouve HM]] |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Hydrogen peroxide]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Nadp]]
| + | |
| - | [[Category: Oxidation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| Structural highlights
Function
CATA_PROMI Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
BACKGROUND: Heme oxidative degradation has been extensively investigated in peroxidases but not in catalases. The verdoheme formation, a product of heme oxidation which inactivates the enzyme, was studied in Proteus mirabilis catalase. METHODS: The verdoheme was generated by adding peracetic acid and analyzed by mass spectrometry and spectrophotometry. RESULTS: Kinetics follow-up of different catalase reactional intermediates shows that i) the formation of compound I always precedes that of verdoheme, ii) compound III is never observed, iii) the rate of compound II decomposition is not compatible with that of verdoheme formation, and iv) dithiothreitol prevents the verdoheme formation but not that of compound II, whereas NADPH prevents both of them. The formation of verdoheme is strongly inhibited by EDTA but not increased by Fe3+ or Cu2+ salts. The generation of verdoheme is facilitated by the presence of protein radicals as observed in the F194Y mutated catalase. The inability of the inactive variant (H54F) to form verdoheme, indicates that the heme oxidation is fully associated to the enzyme catalysis. CONCLUSION: These data, taken together, strongly suggest that the verdoheme formation pathway originates from compound I rather than from compound II. GENERAL SIGNIFICANCE: The autocatalytic verdoheme formation is likely to occur in vivo.
Verdoheme formation in Proteus mirabilis catalase.,Andreoletti P, Mouesca JM, Gouet P, Jaquinod M, Capeillere-Blandin C, Jouve HM Biochim Biophys Acta. 2009 Aug;1790(8):741-53. Epub 2009 Apr 24. PMID:19394409[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Andreoletti P, Mouesca JM, Gouet P, Jaquinod M, Capeillere-Blandin C, Jouve HM. Verdoheme formation in Proteus mirabilis catalase. Biochim Biophys Acta. 2009 Aug;1790(8):741-53. Epub 2009 Apr 24. PMID:19394409 doi:10.1016/j.bbagen.2009.04.010
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