deMaré F, Kurtz D M, Nordlund P
Department of Molecular Biology, Stockholm University, Sweden.
Nat Struct Biol. 1996 Jun;3(6):539-46. doi: 10.1038/nsb0696-539.
We have determined the structure of rubrerythrin, a non-haem iron protein from the anaerobic sulphate-reducing bacterium, Desulfovibrio vulgaris (Hildenborough), by X-ray crystallography. The structure reveals a tetramer of two-domain subunits. Each subunit contains a four-helix bundle surrounding a diiron-oxo site and a C-terminal rubredoxin-like FeS4 domain. The diiron-oxo site contains a larger number of carboxylate ligands and a higher degree of solvent exposure than do those in other diiron-oxo proteins. The four-helix bundle of rubrerythrin closely resembles those of the ferritin and bacterioferritin subunits, suggesting a relationship among these proteins-consistent with the recently demonstrated ferroxidase activity of rubrerythrin.
我们通过X射线晶体学确定了来自厌氧硫酸盐还原菌嗜热栖热放线菌（Hildenborough）的非血红素铁蛋白红氧还蛋白的结构。该结构揭示了由两个结构域亚基组成的四聚体。每个亚基包含围绕一个双铁-氧位点的四螺旋束和一个C端类红氧还蛋白FeS4结构域。与其他双铁-氧蛋白相比，双铁-氧位点含有更多数量的羧酸盐配体，且溶剂暴露程度更高。红氧还蛋白的四螺旋束与铁蛋白和细菌铁蛋白亚基的四螺旋束非常相似，这表明这些蛋白质之间存在一种关系，这与最近证明的红氧还蛋白的铁氧化酶活性一致。
