STRUCTURE, FUNCTION, AND EVOLUTION OF FERRITINS
STRUCTURE, FUNCTION, AND EVOLUTION OF FERRITINS
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DOI：
10.1016/0162-0134(92)84062-r
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发表时间：
1992-08-15
影响因子：
3.9
通讯作者：
YEWDALL, SJ
中科院分区：
文献类型：
--
作者：
ANDREWS, SC;AROSIO, P;YEWDALL, SJ
动植物铁蛋白和细菌铁蛋白具有共同的铁储存功能，尽管它们在细胞定位和生物合成调控方面存在差异。植物铁蛋白和BFR在一级结构和铁氧化酶中心残基的保守性方面更类似于哺乳动物的H链而不是哺乳动物的L链。因此，它们可能起源于一个共同的H型祖先。最近在E.第二种类型的铁储存蛋白（FTN）类似于铁蛋白H链的大肠杆菌提出了这两种蛋白质在这种生物体中的相对作用是什么的问题。哺乳动物L铁蛋白缺乏铁氧化酶中心，形成一个独特的组。哺乳动物和无脊椎动物铁蛋白的三维结构的比较，以及植物铁蛋白和BFR的计算机建模，表明一个很好的保守的分子框架。许多铁蛋白均聚物变体的表征已经允许鉴定参与铁摄取的一些残基和调查哺乳动物H和L链之间的一些功能差异。
The ferritins of animals and plants and the bacterioferritins (BFRs) have a common iron-storage function in spite of differences in cytological location and biosynthetic regulation. The plant ferritins and BFRs are more similar to the H chains of mammals than to mammalian L chains, with respect to primary structure and conservation of ferroxidase center residues. Hence they probably arose from a common H-type ancestor. The recent discovery in E. coli of a second type of iron-storage protein (FTN) resembling ferritin H chains raises the question of what the relative roles of these two proteins are in this organism. Mammalian L ferritins lack ferroxidase centers and form a distinct group. Comparison of the three-dimensional structures of mammalian and invertebrate ferritins, as well as computer modeling of plant ferritins and of BFR, indicate a well conserved molecular framework. The characterisation of numerous ferritin homopolymer variants has allowed the identification of some of the residues involved in iron uptake and an investigation of some of the functional differences between mammalian H and L chains.