Manganese peroxidase

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{{STRUCTURE_3m5q| PDB=3m5q | SIZE=400| SCENE= |right|CAPTION=Heme-containing glycosylated manganese peroxidase complex with glycerol, Mn+2 (purple) and Ca+2 (green) ions [[3m5q]] }}
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<StructureSection load='3m5q' size='450' side='right' scene='48/486477/Cv/1' caption='Heme-containing glycosylated manganese peroxidase complex with glycerol, Mn+2 (purple) and Ca+2 (green) ions [[3m5q]]'>
== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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The Mn binding site of MnP contains the heme group which coordinates with the ion. The heme group is coordinated mostly by aromatic side chains<ref>PMID:20356630</ref>.
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The <scene name='48/486477/Cv/7'>Mn binding site of MnP contains the heme group which coordinates with the ion</scene>. Water molecules are shown as red spheres. The <scene name='48/486477/Cv/8'>heme group is coordinated mostly by aromatic side chains</scene><ref>PMID:20356630</ref>.
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</StructureSection>
==3D structures of manganese peroxidase==
==3D structures of manganese peroxidase==

Current revision

Heme-containing glycosylated manganese peroxidase complex with glycerol, Mn+2 (purple) and Ca+2 (green) ions 3m5q

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3D structures of manganese peroxidase

Updated on 09-July-2019

References

  1. Youngs HL, Sundaramoorthy M, Gold MH. Effects of cadmium on manganese peroxidase competitive inhibition of MnII oxidation and thermal stabilization of the enzyme. Eur J Biochem. 2000 Mar;267(6):1761-9. PMID:10712608
  2. Sundaramoorthy M, Gold MH, Poulos TL. Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. J Inorg Biochem. 2010 Jun;104(6):683-90. Epub 2010 Mar 6. PMID:20356630 doi:10.1016/j.jinorgbio.2010.02.011

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Michal Harel, Alexander Berchansky

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