2L18
An arsenate reductase in the phosphate binding state
2L18 の概要
| エントリーDOI | 10.2210/pdb2l18/pdb |
| 関連するPDBエントリー | 2L17 2L19 |
| 分子名称 | Arsenate reductase (1 entity in total) |
| 機能のキーワード | alpha/beta sandwich, oxidoreductase |
| 由来する生物種 | Synechocystis |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14739.71 |
| 構造登録者 | |
| 主引用文献 | Yu, C.,Xia, B.,Jin, C. (1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803 Biomol.Nmr Assign., 5:85-87, 2011 Cited by PubMed Abstract: Arsenate reductases (ArsC) are a group of enzymes that play essential roles in biological arsenic detoxification pathways by catalyzing the intracellular reduction of arsenate to arsenite, which is subsequently extruded from the cells by specific transport systems. The ArsC protein from cyanobacterium Synechocystis sp. strain PCC 6803 (SynArsC) is related to the thioredoxin-dependent ArsC family, but uses the glutathione/glutaredoxin system for arsenate reduction. Therefore, it is classified to a novel thioredoxin/glutaredoxin hybrid arsenate reductase family. Herein we report the chemical shift assignments of (1)H, (13)C and (15)N atoms for the reduced form of SynArsC, which provides a starting point for further structural analysis and elucidation of its enzymatic mechanism. PubMed: 20960080DOI: 10.1007/s12104-010-9273-2 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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