3M8M

1.05 A Structure of Manganese-free Manganese Peroxidase

3M8M の概要

• エントリーDOI: 10.2210/pdb3m8m/pdb
• 関連するPDBエントリー: 1MNP 1YYD 1YZP 3M5Q
• 分子名称: Manganese peroxidase 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (7 entities in total)
• 機能のキーワード: peroxidase, heme, mn(ii)-binding site, ca(ii)-binding site, glycosylation, high resolution, calcium, disulfide bond, glycoprotein, hydrogen peroxide, iron, lignin degradation, manganese, metal-binding, oxidoreductase, secreted
• 由来する生物種: Phanerochaete chrysosporium (White-rot fungus)
• 細胞内の位置: Secreted: Q02567
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38968.36

構造登録者

Sundaramoorthy, M.,Gold, M.H.,Poulos, T.L. (登録日: 2010-03-18, 公開日: 2010-04-14, 最終更新日: 2024-10-09)

主引用文献

Sundaramoorthy, M.,Gold, M.H.,Poulos, T.L.
Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism.
J.Inorg.Biochem., 104:683-690, 2010

PubMed Abstract: 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.

PubMed: 20356630
DOI: 10.1016/j.jinorgbio.2010.02.011

実験手法

X-RAY DIFFRACTION (1.05 Å)