2.6 A resolution crystal structure of the bacterioferritin from Azotobacter vinelandii.
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.
Liu
He-Li
HL
Institute of Biophysics, Chinese Academy of Sciences, Datun Road 15, Chaoyang District, Beijing 100101, China.
Zhou
Hui-Na
HN
Xing
Wei-Man
WM
Zhao
Jian-Feng
JF
Li
Shu-Xing
SX
Huang
Ju-Fu
JF
Bi
Ru-Chang
RC
D016948:Azotobacter vinelandii / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D003573:Cytochrome b Group / Q000737:chemistry* / Q000378:metabolism; D005293:Ferritins / Q000737:chemistry* / Q000378:metabolism; D006418:Heme / Q000737:chemistry; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009068:Movement
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D006418:Heme; D005293:Ferritins; C018032:bacterioferritin; D007501:Iron