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. 2017 Apr 10;45(9):5013–5025. doi: 10.1093/nar/gkx230

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© The Author(s) 2017. 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-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 7. — Structural comparison of mouse RNase 1 and CdiA-CT^Ykris. For the three panels, Cartoon representation depicts CdiA-CT^Ykris (green) and mouse RNase 1 (white, PDB code: 3TSR) with disulfide bonds represented in sticks with carbon and sulfur atoms colored white and yellow, respectively. (A) The Cys27–Cys85 bond in RNase 1 (left) is substituted by hydrophobic interactions in CdiA-CT^Ykris (right). (B) Superimposition of RNase 1 and CdiA-CT^Ykris. The disulfide bond between Cys41 and Cys96 in RNase 1 is replaced by an α-helix in CdiA-CT^Ykris. (C) RNase 1 has an extended loop that is stabilized by Cys58–Cys111 and Cys66–Cys73 linkages (left). This loop region is substituted with a fourth α-helix in the CdiA-CT^Ykris structure (right).