1mn1
From Proteopedia
(New page: 200px<br /><applet load="1mn1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mn1, resolution 2.0Å" /> '''MANGANESE PEROXIDASE ...) |
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| - | [[Image:1mn1.jpg|left|200px]]<br /><applet load="1mn1" size=" | + | [[Image:1mn1.jpg|left|200px]]<br /><applet load="1mn1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mn1, resolution 2.0Å" /> | caption="1mn1, resolution 2.0Å" /> | ||
'''MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N'''<br /> | '''MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Manganese peroxidase (MnP), an extracellular heme enzyme from the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1MN1 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:// | + | 1MN1 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 <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=HEM:'>HEM</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1MN1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Phanerochaete chrysosporium]] | [[Category: Phanerochaete chrysosporium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Poulos, T | + | [[Category: Poulos, T L.]] |
[[Category: Sundaramoorthy, M.]] | [[Category: Sundaramoorthy, M.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:00 2008'' |
Revision as of 11:57, 21 February 2008
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MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT D179N
Overview
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.
About this Structure
1MN1 is a Single protein structure of sequence from Phanerochaete chrysosporium with and as ligands. Active as Manganese peroxidase, with EC number 1.11.1.13 Full crystallographic information is available from OCA.
Reference
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
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