1mn1

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{{Seed}}
 
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[[Image:1mn1.png|left|200px]]
 
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==MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N==
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The line below this paragraph, containing "STRUCTURE_1mn1", creates the "Structure Box" on the page.
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<StructureSection load='1mn1' size='340' side='right'caption='[[1mn1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1mn1| PDB=1mn1 | SCENE= }}
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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=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>
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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/1mn1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1mn1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N===
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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:9211904<ref>PMID:9211904</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1mn1" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_9211904}}, adds the Publication Abstract to the page
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*[[Manganese peroxidase|Manganese peroxidase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 9211904 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_9211904}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1MN1 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MN1 OCA].
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[[Category: Phanerodontia chrysosporium]]
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[[Category: Poulos TL]]
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==Reference==
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[[Category: Sundaramoorthy M]]
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<ref group="xtra">PMID:9211904</ref><references group="xtra"/>
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[[Category: Manganese peroxidase]]
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[[Category: Phanerochaete chrysosporium]]
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[[Category: Poulos, T L.]]
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[[Category: Sundaramoorthy, M.]]
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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://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:55:18 2009''
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Current revision

MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N

PDB ID 1mn1

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