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. 2019 Jul 1;47(14):7690–7702. doi: 10.1093/nar/gkz563

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© The Author(s) 2019. 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 Non-Commercial 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 2. — Interactions within and between two heterodimers of the RHH antitoxin KacA. (A) Overall structure of two KacA heterodimers viewed from the top. The interactions within and between the two KacA heterodimers identified by the dashed line boxes (I, II and III) are detailed in panels (B–E). Residues participating in the interface are drawn in stick representation and labelled in all figures. Hydrogen bonds are indicated by black dashed lines in all figures. (B) Superposition of two antitoxins in alternate conformations. (C) Details of the interactions at site I of the RHH domain shown in two views with 180 rotation along the horizontal axis. (D) Details of the interactions at site II, showing the interactions between KacA1 and KacA2′. (E) Details of the interactions at site III, showing the interactions between KacA1 and KacA2.