Liu He-Li, Zhou Hui-Na, Xing Wei-Man, Zhao Jian-Feng, Li Shu-Xing, Huang Ju-Fu, Bi Ru-Chang
Institute of Biophysics, Chinese Academy of Sciences, Datun Road 15, Chaoyang District, Beijing 100101, China.
FEBS Lett. 2004 Aug 27;573(1-3):93-8. doi: 10.1016/j.febslet.2004.07.054.
The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 A resolution. Both the low occupancy of one iron ion in the dinuclear iron center and the deviation of its adjacent residue His130 from the center suggest migration of the iron ion from the dinuclear iron site to the inner nucleation site. The concerted movement of His130 and Glu47 may admit a dynamic gating mechanism for shift of the oxidized iron ion. Ba2+ binding to the fourfold channel implicates that the channel bears Fe2+ conductivity and selectivity to provide a route for iron access to the inner cavity during core formation.
已经以2.6埃的分辨率确定了来自棕色固氮菌的细菌铁蛋白的晶体结构。双核铁中心中一个铁离子的低占有率及其相邻残基His130偏离中心，这表明铁离子从双核铁位点迁移到内部成核位点。His130和Glu47的协同运动可能允许氧化态铁离子转移的动态门控机制。Ba2+与四重通道结合表明该通道具有Fe2+传导性和选择性，以在核心形成过程中为铁进入内腔提供一条途径。
