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| | ==MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N== | | ==MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N== |
| - | <StructureSection load='1mn1' size='340' side='right' caption='[[1mn1]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1mn1' size='340' side='right'caption='[[1mn1]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1mn1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chrysosporium_pruinosum_(gilman_&_abbott)_carmich. Chrysosporium pruinosum (gilman & abbott) carmich.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MN1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MN1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1mn1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phanerodontia_chrysosporium Phanerodontia chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MN1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MNP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5306 Chrysosporium pruinosum (Gilman & Abbott) Carmich.])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Manganese_peroxidase Manganese peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.13 1.11.1.13] </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=1mn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mn1 OCA], [https://pdbe.org/1mn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mn1 RCSB], [https://www.ebi.ac.uk/pdbsum/1mn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mn1 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mn1 OCA], [http://pdbe.org/1mn1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mn1 RCSB], [http://www.ebi.ac.uk/pdbsum/1mn1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mn1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEM1_PHACH PEM1_PHACH]] Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds. | + | [https://www.uniprot.org/uniprot/PEM1_PHACH PEM1_PHACH] Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/1mn1_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/1mn1_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Manganese peroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Poulos, T L]] | + | [[Category: Phanerodontia chrysosporium]] |
| - | [[Category: Sundaramoorthy, M]] | + | [[Category: Poulos TL]] |
| - | [[Category: Donor: h2o2 oxidoreductase]] | + | [[Category: Sundaramoorthy M]] |
| - | [[Category: Heme enzyme]]
| + | |
| - | [[Category: Peroxidase]]
| + | |
| Structural highlights
Function
PEM1_PHACH Catalyzes the oxidation of Mn(2+) to Mn(3+). The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin compounds.
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
Manganese peroxidase (MnP), an extracellular heme enzyme from the lignin-degrading basidiomycetous fungus, Phanerochaete chrysosporium, catalyzes the oxidation of MnII to MnIII. The latter, acting as a diffusible redox mediator, is capable of oxidizing a variety of lignin model compounds. The proposed MnII binding site of MnP consists of a heme propionate, three acidic ligands (Glu-35, Glu-39, and Asp-179), and two water molecules. Using crystallographic methods, this binding site was probed by altering the amount of MnII bound to the protein. Crystals grown in the absence of MnII, or in the presence of EDTA, exhibited diminished electron density at this site. Crystals grown in excess MnII exhibited increased electron density at the proposed binding site but nowhere else in the protein. This suggests that there is only one major MnII binding site in MnP. Crystal structures of a single mutant (D179N) and a double mutant (E35Q,D179N) at this site were determined. The mutant structures lack a cation at the MnII binding site. The structure of the MnII binding site is altered significantly in both mutants, resulting in increased access to the solvent and substrate.
Crystal structures of substrate binding site mutants of manganese peroxidase.,Sundaramoorthy M, Kishi K, Gold MH, Poulos TL J Biol Chem. 1997 Jul 11;272(28):17574-80. PMID:9211904[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sundaramoorthy M, Kishi K, Gold MH, Poulos TL. Crystal structures of substrate binding site mutants of manganese peroxidase. J Biol Chem. 1997 Jul 11;272(28):17574-80. PMID:9211904
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