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. 2016 Nov 8;7:13248. doi: 10.1038/ncomms13248

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Copyright © 2016, The Author(s)

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The FeS cluster domain, anchored to NBD1 via a two β-strand lever arm, swings out of the NBD cleft and converges towards the 30S subunit to occupy a cleft between the S12 r-protein and rRNA (h44) of the small ribosomal subunit. Due to this conformation change, the Cα–Cα distance between these highly conserved lysines in Archaea, yeast and human is reduced from 59.5 Å in the pre-splitting state to 17.5 Å in the post-recycling state.