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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus.
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X-ray structure of a soluble Rieske-type ferredoxin from Mus musculus.

机译：可溶性Rieske-type x射线结构ferredoxin from惹不起musculus。

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摘要

The 2.07 A resolution X-ray crystal structure of a soluble Rieske-type ferredoxin from Mus musculus encoded by the gene Mm.266515 is reported. Although they are present as covalent domains in eukaryotic membrane oxidase complexes, soluble Rieske-type ferredoxins have not previously been observed in eukaryotes. The overall structure of the mouse Rieske-type ferredoxin is typical of this class of iron-sulfur proteins and consists of a larger partial beta-barrel domain and a smaller domain containing Cys57, His59, Cys80 and His83 that binds the [2Fe-2S] cluster. The S atoms of the cluster are hydrogen-bonded by six backbone amide N atoms in a pattern typical of membrane-bound high-potential eukaryotic respiratory Rieske ferredoxins. However, phylogenetic analysis suggested that the mouse Rieske-type ferredoxin was more closely related to bacterial Rieske-type ferredoxins. Correspondingly, the structure revealed an extended loop most similar to that seen in Rieske-type ferredoxin subunits of bacterial aromatic dioxygenases, including the positioning of an aromatic side chain (Tyr85) between this loop and the [2Fe-2S] cluster. The mouse Rieske-type ferredoxin was shown to be capable of accepting electrons from both eukaryotic and prokaryotic oxidoreductases, although it was unable to serve as an electron donor for a bacterial monooxygenase complex. The human homolog of mouse Rieske-type ferredoxin was also cloned and purified. It behaved identically to mouse Rieske-type ferredoxin in all biochemical characterizations but did not crystallize. Based on its high sequence identity, the structure of the human homolog is likely to be modeled well by the mouse Rieske-type ferredoxin structure.
机译：2.07分辨率x射线晶体结构从亩骶可溶性Rieske-type铁氧还蛋白编码的基因Mm.266515报道。尽管他们存在的共价域真核细胞膜氧化酶复合物,可溶性Rieske-type铁氧还蛋白以前没有真核生物中观察到。鼠标Rieske-type铁氧还蛋白是典型的这类iron-sulfur蛋白质,由一个更大的部分beta-barrel域和一个较小的域包含Cys57 His59, Cys80和His83将[2 fe-2s)集群。集群的原子是由六个氢键骨干酰胺N原子的典型模式膜结合高潜力的真核呼吸Rieske铁氧还蛋白。系统发育分析显示,鼠标Rieske-type铁氧还蛋白更密切相关对细菌Rieske-type铁氧还蛋白。相应地,透露一个结构延长循环最类似的Rieske-type铁氧还蛋白亚基的细菌芳香加双氧酶,包括定位芳香的侧链(Tyr85)之间循环和[2 fe-2s)集群。Rieske-type铁氧还蛋白被证明有能力真核和接受电子原核的氧化还原酶,尽管它无法作为一个电子供体细菌单氧酶复杂。同族体鼠标Rieske-type铁氧还蛋白也克隆和纯化。在所有生化鼠标Rieske-type铁氧还蛋白特征,但没有结晶。在其高序列的身份,的结构人类的同族体可能通过建模鼠标Rieske-type铁氧还蛋白结构。

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