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2.6 Å resolution crystal structure of the bacterioferritin from Azotobacter vinelandii
Author(s) -
Liu He-Li,
Zhou Hui-Na,
Xing Wei-Man,
Zhao Jian-Feng,
Li Shu-Xing,
Huang Ju-Fu,
Bi Ru-Chang
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.054
Subject(s) - azotobacter vinelandii , chemistry , crystallography , ion , ferrous , stereochemistry , nitrogen , nitrogenase , organic chemistry , nitrogen fixation
The crystal structure of the bacterioferritin from Azotobacter vinelandii has been determined at 2.6 Å 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. Ba 2+ binding to the fourfold channel implicates that the channel bears Fe 2+ conductivity and selectivity to provide a route for iron access to the inner cavity during core formation.