Zhejiang Collaborative Innovation Center for High Value Utilization of Byproducts from Ethylene Project, Ningbo Polytechnic, Ningbo, Zhejiang, 315800, China.
State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, Zhejiang, 315211, China; School of Marine Science, Ningbo University, Ningbo, Zhejiang, 315823, China.
Biochem Biophys Res Commun. 2020 Mar 26;524(1):217-223. doi: 10.1016/j.bbrc.2020.01.069. Epub 2020 Jan 23.
Ferritins are ubiquitous iron-binding proteins that are mainly related to iron storage, detoxification and innate immunity. Here, we present the crystal structure of a marine invertebrate ferritin from Sinonovacula constricta at a resolution of 1.98 Å. The S. constricta ferritin (ScFer) possessed some structural similarities with vertebrate ferritins, and they shared a well-conserved architecture composed of five α-helical bundles that assembled into a cage-like structure with 24-subunits. The structure of ScFer also showed iron binding sites in the 3-fold channel, ferroxidase center, and putative nucleation sites. Further, electrostatic potential calculations suggested that the electrostatic gradient of the 3-fold channel could provide a guidance mechanism for iron entering the ferritin cavity.
铁蛋白是一种广泛存在的铁结合蛋白，主要与铁储存、解毒和先天免疫有关。在这里，我们呈现了来自中国蛤蜊（Sinonovacula constricta）的海洋无脊椎动物铁蛋白的晶体结构，分辨率为 1.98 Å。该中国蛤蜊铁蛋白（ScFer）与脊椎动物铁蛋白具有一些结构相似性，它们共享由五个α-螺旋束组成的高度保守的结构，组装成具有 24 个亚基的笼状结构。ScFer 的结构还显示了 3 倍通道、亚铁氧化酶中心和潜在的成核位点的铁结合位点。此外，静电势计算表明，3 倍通道的静电梯度可以为铁进入铁蛋白腔提供一种导向机制。
