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1mn2

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(New page: 200px<br /><applet load="1mn2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mn2, resolution 2.0&Aring;" /> '''MANGANESE PEROXIDASE ...)
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[[Image:1mn2.jpg|left|200px]]<br /><applet load="1mn2" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mn2, resolution 2.0&Aring;" />
 
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'''MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT E35Q, D179N'''<br />
 
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==Overview==
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==MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT E35Q, D179N==
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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.
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<StructureSection load='1mn2' size='340' side='right'caption='[[1mn2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mn2]] 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=1MN2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MN2 FirstGlance]. <br>
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</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&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mn2 OCA], [https://pdbe.org/1mn2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mn2 RCSB], [https://www.ebi.ac.uk/pdbsum/1mn2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mn2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mn/1mn2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mn2 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1MN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium] with CA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MN2 OCA].
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*[[Manganese peroxidase|Manganese peroxidase]]
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9211904 9211904]
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[[Category: Large Structures]]
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[[Category: Manganese peroxidase]]
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[[Category: Phanerodontia chrysosporium]]
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[[Category: Phanerochaete chrysosporium]]
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[[Category: Poulos TL]]
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[[Category: Single protein]]
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[[Category: Sundaramoorthy M]]
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[[Category: Poulos, T.L.]]
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[[Category: Sundaramoorthy, M.]]
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[[Category: CA]]
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[[Category: HEM]]
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[[Category: donor: h2o2 oxidoreductase]]
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[[Category: heme enzyme]]
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[[Category: peroxidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:32:32 2007''
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Current revision

MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT E35Q, D179N

PDB ID 1mn2

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