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| | <StructureSection load='1e93' size='340' side='right'caption='[[1e93]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1e93' size='340' side='right'caption='[[1e93]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1e93]] 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=1E93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E93 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1e93]] 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=1E93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E93 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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]] 2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OMT:S-DIOXYMETHIONINE'>OMT</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OMT:S-DIOXYMETHIONINE'>OMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2cae|2cae]], [[2caf|2caf]], [[2cag|2cag]], [[2cah|2cah]]</div></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=1e93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e93 OCA], [https://pdbe.org/1e93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e93 RCSB], [https://www.ebi.ac.uk/pdbsum/1e93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e93 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=1e93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e93 OCA], [https://pdbe.org/1e93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e93 RCSB], [https://www.ebi.ac.uk/pdbsum/1e93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e93 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: Andreoletti, P]] | + | [[Category: Proteus mirabilis]] |
| - | [[Category: Gagnon, J]] | + | [[Category: Andreoletti P]] |
| - | [[Category: Jaquinod, M]] | + | [[Category: Gagnon J]] |
| - | [[Category: Jouve, H M]] | + | [[Category: Jaquinod M]] |
| - | [[Category: Sainz, G]] | + | [[Category: Jouve HM]] |
| - | [[Category: Hem]]
| + | [[Category: Sainz G]] |
| - | [[Category: Hydrogen peroxide]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Nadp]]
| + | |
| - | [[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
Heme catalases are homotetrameric enzymes with a highly conserved complex quaternary structure, and their functional role is still not well understood. Proteus mirabilis catalase (PMC), a heme enzyme belonging to the family of NADPH-binding catalases, was efficiently overexpressed in E. coli. The recombinant catalase (rec PMC) was deficient in heme with one-third heme and two-thirds protoporphyrin IX as determined by mass spectrometry and chemical methods. This ratio was influenced by the expression conditions, but the enzyme-specific activity calculated relative to the heme content remained unchanged. The crystal structure of rec PMC was solved to a resolution of 2.0 A, the highest resolution obtained to date with PMC. The overall structure was quite similar to that of wild-type PMC, and it is surprising that the absence of iron had no effect on the structure of the active site. Met 53 close to the essential His 54 was found less oxidized in rec PMC than in the wild-type enzyme. An acetate anion was modeled in an anionic pocket, away from the heme group but important for the enzymatic reaction. An alternate conformation observed for Arg 99 could play a role in the formation of the H-bond network connecting two symmetrical subunits of the tetramer.
High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron.,Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM Proteins. 2003 Feb 1;50(2):261-71. PMID:12486720[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Andreoletti P, Sainz G, Jaquinod M, Gagnon J, Jouve HM. High-resolution structure and biochemical properties of a recombinant Proteus mirabilis catalase depleted in iron. Proteins. 2003 Feb 1;50(2):261-71. PMID:12486720 doi:10.1002/prot.10283
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