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| | == Structural highlights == | | == Structural highlights == |
| | <table><tr><td colspan='2'>[[1nm0]] 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=1NM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NM0 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1nm0]] 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=1NM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NM0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <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='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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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;'>[[1m85|1m85]], [[1mqf|1mqf]], [[2cag|2cag]], [[2cah|2cah]], [[1e93|1e93]]</div></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=1nm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm0 OCA], [https://pdbe.org/1nm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1nm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nm0 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=1nm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nm0 OCA], [https://pdbe.org/1nm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1nm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nm0 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: Catalase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Proteus mirabilis]] | | [[Category: Proteus mirabilis]] |
| - | [[Category: Andreoletti, P]] | + | [[Category: Andreoletti P]] |
| - | [[Category: Gouet, P]] | + | [[Category: Gouet P]] |
| - | [[Category: Jouve, H M]] | + | [[Category: Jouve HM]] |
| - | [[Category: Pernoud, A]] | + | [[Category: Pernoud A]] |
| - | [[Category: Alpha+beta]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
1nm0 is a 1 chain structure with sequence from Proteus mirabilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.3Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
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
The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction.
Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid.,Andreoletti P, Pernoud A, Sainz G, Gouet P, Jouve HM Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2163-8. Epub 2003, Nov 27. PMID:14646074[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Andreoletti P, Pernoud A, Sainz G, Gouet P, Jouve HM. Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2163-8. Epub 2003, Nov 27. PMID:14646074
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