State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, Zhejiang, 315211, China; College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, Zhejiang, 315823, China.
College of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, Zhejiang, 315823, China.
Biochem Biophys Res Commun. 2020 Oct 15;531(2):195-202. doi: 10.1016/j.bbrc.2020.07.069. Epub 2020 Aug 10.
Ferritin is an important hub of iron metabolism because it stores iron during times of iron overload and releases iron during iron deficiency. Here, we present the first crystal structure of ferritin from the marine invertebrate Dendrorhynchus zhejiangensis with a 2.3 Å resolution. D. zhejiangensis ferritin (DzFer) exhibits a common cage-shaped hollow sphere with 24 subunits containing the ferroxidase centers and 3-fold and 4-fold channels. The structure of DzFer shows highly conserved catalytic residues in the ferroxidase center. The metal wire formed by ferrous ions in the 3-fold channel reveals the path that iron ions use to enter and translocate into the ferroxidase site to be oxidized and finally arrive at the nucleation site. However, the electrostatic environment of the channels and pores exhibits significant and extensive variability, suggesting that ferritins execute diverse functions in different environments.
铁蛋白是铁代谢的重要枢纽，因为它在铁过载时储存铁，在缺铁时释放铁。在这里，我们呈现了来自海洋无脊椎动物浙江文昌鱼的铁蛋白的首个晶体结构，分辨率为 2.3Å。浙江文昌鱼铁蛋白（DzFer）呈现出常见的笼形空心球体，由 24 个亚基组成，包含亚铁氧化酶中心和 3 倍和 4 倍通道。DzFer 的结构显示了亚铁氧化酶中心中高度保守的催化残基。3 倍通道中由亚铁离子形成的金属丝揭示了铁离子进入并转移到亚铁氧化酶位点被氧化并最终到达成核位点的途径。然而，通道和孔的静电环境表现出显著和广泛的可变性，表明铁蛋白在不同环境中执行不同的功能。
