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. 2022 Apr 12;50(8):4713–4731. doi: 10.1093/nar/gkac228

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© The Author(s) 2022. 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 (https://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 6. — Structure of CdiA–CT:CdiI^EC869 complexed with Tu. (A) Stereoview of the structure of the CdiA–CT:CdiI:Tu complex. CdiA–CT^EC869, CdiI^EC869 and Tu are colored cyan, magenta, and yellow, respectively. The modeled CdiA–CT^EC869 contains residues 175–285 (numbered from Val1 of the VENN peptide motif, Supplementary Figure S13A), and the modeled CdiI^EC869 contains residues 3–179. The modeled Tu contains residues 10–393. (B) Stereoview of CdiA–CT^EC869. (C) Stereoview of CdiI^EC869. (D) CdiA–CT^EC869 adopts the BECR fold as observed in other CdiA–CTs targeting the 3′-acceptor region of tRNAs. CdiA–CT^NC101 (blue) from E. coli NC101 (14), CdiA–CT^Kp342 (yellow) from Klebsiella pneumoniae, and CdiA–CT^EC3006 (magenta) from E. coli 3006 (16). (E), (F) Interaction between CdiA–CT (cyan) and domain II of Tu (yellow). (G) Superimposition of the structure of CdiA–CT^EC869:Tu onto that of CdiA–CT^NC101:Tu (14). For clarity, the structures of domain I of Tu in both complex structures are omitted. CdiA–CT^EC869 and domains II/III of Tu in the structure of CdiA–CT^EC869:Tu are colored cyan and yellow, respectively. CdiA–CT^NC101 and domains II/III of Tu in the structure of CdiA–CT^NC101:Tu are colored blue and orange, respectively.