View source for 3m8m


==1.05 A Structure of Manganese-free Manganese Peroxidase==
<StructureSection load='3m8m' size='340' side='right'caption='[[3m8m]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3m8m]] is a 1 chain structure with 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=3M8M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M8M 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yyd|1yyd]], [[1mnp|1mnp]], [[1yzp|1yzp]], [[3m5q|3m5q]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3m8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m8m OCA], [http://pdbe.org/3m8m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m8m RCSB], [http://www.ebi.ac.uk/pdbsum/3m8m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m8m ProSAT]</span></td></tr>
</table>
== 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. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m8/3m8m_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=3m8m ConSurf].
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== Publication Abstract from PubMed ==
Manganese peroxidase (MnP) is an extracellular heme enzyme produced by the lignin-degrading white-rot fungus Phanerochaete chrysosporium. MnP catalyzes the peroxide-dependent oxidation of Mn(II) to Mn(III). The Mn(III) is released from the enzyme in complex with oxalate, enabling the oxalate-Mn(III) complex to serve as a diffusible redox mediator capable of oxidizing lignin, especially under the mediation of unsaturated fatty acids. One heme propionate and the side chains of Glu35, Glu39 and Asp179 have been identified as Mn(II) ligands in our previous crystal structures of native MnP. In our current work, new 0.93A and 1.05A crystal structures of MnP with and without bound Mn(II), respectively, have been solved. This represents only the sixth structure of a protein of this size at 0.93A resolution. In addition, this is the first structure of a heme peroxidase from a eukaryotic organism at sub-Angstrom resolution. These new structures reveal an ordering/disordering of the C-terminal loop, which is likely required for Mn binding and release. In addition, the catalytic Arg42 residue at the active site, normally thought to function only in the peroxide activation process, also undergoes ordering/disordering that is coupled to a transient H-bond with the Mn ligand, Glu39. Finally, these high-resolution structures also reveal the exact H atoms in several parts of the structure that are relevant to the catalytic mechanism.

Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism.,Sundaramoorthy M, Gold MH, Poulos TL J Inorg Biochem. 2010 Jun;104(6):683-90. Epub 2010 Mar 6. PMID:20356630<ref>PMID:20356630</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Manganese peroxidase|Manganese peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Manganese peroxidase]]
[[Category: Phanerochaete chrysosporium]]
[[Category: Gold, M H]]
[[Category: Poulos, T L]]
[[Category: Sundaramoorthy, M]]
[[Category: Calcium]]
[[Category: Disulfide bond]]
[[Category: Glycoprotein]]
[[Category: Glycosylation]]
[[Category: Heme]]
[[Category: High resolution]]
[[Category: Hydrogen peroxide]]
[[Category: Iron]]
[[Category: Lignin degradation]]
[[Category: Manganese]]
[[Category: Metal-binding]]
[[Category: Oxidoreductase]]
[[Category: Peroxidase]]
[[Category: Secreted]]