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Structure and Function of the FeoB G-Domain from Methanococcus jannaschii

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Köster,  Stefan
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Yildiz,  Özkan       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Köster, S., Wehner, M., Herrmann, C., Kühlbrandt, W., & Yildiz, Ö. (2009). Structure and Function of the FeoB G-Domain from Methanococcus jannaschii. Journal of Molecular Biology, 392(2), 405-419. doi:10.1016/j.jmb.2009.07.020.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D7A1-C
Abstract
FeoB in bacteria and archaea is involved in the uptake of ferrous iron (Fe2+), an important cofactor in biological electron transfer and catalysis. Unlike any other known prokaryotic membrane protein, FeoB contains a GTP-binding domain at its N-terminus. We determined high-resolution X-ray structures of the FeoB G-domain from Methanococcus jannaschii with and without bound GDP or Mg2+-GppNHp. The G-domain forms the same dimer in all three structures, with the nucleotide-binding pockets at the dimer interface, as in the ATP-binding domain of ABC transporters. The G-domain follows the typical fold of nucleotide-binding proteins, with a β-strand inserted in switch I that becomes partially disordered upon GTP binding. Switch II does not contact the nucleotide directly and does not change its conformation in response to the bound nucleotide. Release of the nucleotide causes a rearrangement of loop L6, which we identified as the G5 region of FeoB. Together with the C-terminal helix, this loop may transmit the information about the nucleotide-bound state from the G-domain to the transmembrane region of FeoB.