Abstract
The first crystal structure of a native di-iron center in an iron-storage protein (bacterio)ferritin is reported. The protein, isolated from the anaerobic bacterium Desulfovibrio desulfuricans, has the unique property of having Fe-coproporphyrin III as its heme cofactor. The three-dimensional structure of this bacterioferritin was determined in three distinct catalytic/redox states by X-ray crystallography (at 1.95, 2.05 and 2.35 Å resolution), corresponding to different intermediates of the di-iron ferroxidase site. Conformational changes associated with these intermediates support the idea of a route for iron entry into the protein shell through a pore that passes through the di-iron center. Molecular surface and electrostatic potential calculations also suggest the presence of another ion channel, distant from the channels at the three- and four-fold axes proposed as points of entry for the iron atoms.
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Acknowledgements
This work was supported by PRAXIS XXI and POCTI grants. We thank the ESRF, Grenoble (France) for the provision of synchrotron radiation and for a grant to S.M.
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Macedo, S., Romão, C., Mitchell, E. et al. The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans. Nat Struct Mol Biol 10, 285–290 (2003). https://doi.org/10.1038/nsb909
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DOI: https://doi.org/10.1038/nsb909
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