5A9G
Manganese Superoxide Dismutase from Sphingobacterium sp. T2
5A9G の概要
エントリーDOI | 10.2210/pdb5a9g/pdb |
分子名称 | MANGANESE SUPEROXIDE DISMUTASE, MANGANESE (II) ION (3 entities in total) |
機能のキーワード | oxidoreductase, lignin valorisation, lignin oxidation, manganese superoxide dismutase, sphingobacterium |
由来する生物種 | SPHINGOBACTERIUM SPIRITIVORUM |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 52969.14 |
構造登録者 | Rashid, G.M.M.,Taylor, C.R.,Liu, Y.,Zhang, X.,Rea, D.,Fulop, V.,Bugg, T.D.H. (登録日: 2015-07-21, 公開日: 2015-08-05, 最終更新日: 2024-01-10) |
主引用文献 | Rashid, G.M.,Taylor, C.R.,Liu, Y.,Zhang, X.,Rea, D.,Fulop, V.,Bugg, T.D.H. Identification of Manganese Superoxide Dismutase from Sphingobacterium Sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation. Acs Chem.Biol., 10:2286-, 2015 Cited by PubMed Abstract: The valorization of aromatic heteropolymer lignin is an important unsolved problem in the development of a biomass-based biorefinery, for which novel high-activity biocatalysts are needed. Sequencing of the genomic DNA of lignin-degrading bacterial strain Sphingobacterium sp. T2 revealed no matches to known lignin-degrading genes. Proteomic matches for two manganese superoxide dismutase proteins were found in partially purified extracellular fractions. Recombinant MnSOD1 and MnSOD2 were both found to show high activity for oxidation of Organosolv and Kraft lignin, and lignin model compounds, generating multiple oxidation products. Structure determination revealed that the products result from aryl-Cα and Cα-Cβ bond oxidative cleavage and O-demethylation. The crystal structure of MnSOD1 was determined to 1.35 Å resolution, revealing a typical MnSOD homodimer harboring a five-coordinate trigonal bipyramidal Mn(II) center ligated by three His, one Asp, and a water/hydroxide in each active site. We propose that the lignin oxidation reactivity of these enzymes is due to the production of a hydroxyl radical, a highly reactive oxidant. This is the first demonstration that MnSOD is a microbial lignin-oxidizing enzyme. PubMed: 26198187DOI: 10.1021/ACSCHEMBIO.5B00298 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.35 Å) |
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