The iron superoxide dismutase found in the pathogenic amoeba Acanthamoeba castellanii (AcFeSOD) may play essential roles in the survival of the parasite, not only by protecting it from endogenous oxidative stress but also by detoxifying oxidative killing of the parasite by host immune effector cells. The AcFeSOD protein was expressed in a stable form using an Escherichia coli expression system and was crystallized by the microbatch and hanging‐drop vapour‐diffusion methods. The structure was determined to 2.33 Å resolution from a single AcFeSOD crystal. The crystal belonged to the hexagonal space group P6₁ and contained 12 molecules forming three tetramers in the asymmetric unit, with an iron ion bound in each molecule. Structural comparisons and sequence alignment of AcFeSOD with other FeSODs showed a well conserved overall fold and conserved active‐site residues with subtle differences.

中文翻译：

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来自致病性阿米巴棘阿米巴的铁超氧化物歧化酶的晶体结构。


在致病性阿米巴棘阿米巴( Ac FeSOD) 中发现的铁超氧化物歧化酶可能在寄生虫的生存中发挥重要作用，不仅可以保护其免受内源性氧化应激，还可以通过宿主免疫效应细胞对寄生虫的氧化杀伤进行解毒。 Ac FeSOD 蛋白使用大肠杆菌表达系统以稳定形式表达，并通过微批量和悬滴蒸汽扩散方法进行结晶。单个Ac FeSOD 晶体的结构分辨率为 2.33 Å。该晶体属于六方空间群P 6 ₁ ，包含12个分子，在不对称单元中形成三个四聚体，每个分子中结合有一个铁离子。 Ac FeSOD 与其他 FeSOD 的结构比较和序列比对显示出保守的整体折叠和保守的活性位点残基，但存在细微的差异。