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. 2015 Sep 8;43(19):9529–9540. doi: 10.1093/nar/gkv868

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — The crystal structure of CptIN_Er to 2.2Å resolution. (A) The architecture of the CptIN_Er locus, showing the tandem repeats upstream of the toxic CptN_Er ORF that become processed into CptI_Er monomers. (B) When analysed with symmetry cells in conjunction with data from size exclusion chromatography, the biological unit was found to be a heterotetramer—an oval structure with two protein monomers at the poles (CptN_Er) held together by two pseudoknotted RNAs (CptI_Er). The surface representation shows the electrostatic potential (red: electronegative, blue: electropositive. (PDB: 4RMO) (C) The structural core of the protein is a highly twisted β-sheet surrounded by α-helices. (D) The overlay with carbon-α traces of ToxN_Pa (magenta, PDB: 2XDD) and Kid, a Type II RNase (cyan, PDB: 1M1F), shows the lack of the kinked helix seen in ToxN_Pa in CptN_Er, but still an overall similarity in fold.