1MN2

MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT E35Q, D179N

1MN2 の概要

• エントリーDOI: 10.2210/pdb1mn2/pdb
• 分子名称: MANGANESE PEROXIDASE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: peroxidase, donor: h2o2 oxidoreductase, heme enzyme
• 由来する生物種: Phanerochaete chrysosporium
• 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: 38602.04

構造登録者

Sundaramoorthy, M.,Poulos, T.L. (登録日: 1997-04-26, 公開日: 1997-09-04, 最終更新日: 2024-10-30)

主引用文献

Sundaramoorthy, M.,Kishi, K.,Gold, M.H.,Poulos, T.L.
Crystal structures of substrate binding site mutants of manganese peroxidase.
J.Biol.Chem., 272:17574-17580, 1997

PubMed Abstract: 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.

PubMed: 9211904
DOI: 10.1074/jbc.272.28.17574

実験手法

X-RAY DIFFRACTION (2 Å)