Structural highlights
Function
[BFR_AZOVI] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
2.6 A resolution crystal structure of the bacterioferritin from Azotobacter vinelandii.,Liu HL, Zhou HN, Xing WM, Zhao JF, Li SX, Huang JF, Bi RC FEBS Lett. 2004 Aug 27;573(1-3):93-8. PMID:15327981[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu HL, Zhou HN, Xing WM, Zhao JF, Li SX, Huang JF, Bi RC. 2.6 A resolution crystal structure of the bacterioferritin from Azotobacter vinelandii. FEBS Lett. 2004 Aug 27;573(1-3):93-8. PMID:15327981 doi:10.1016/j.febslet.2004.07.054
