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. 2020 Sep 8;8:797. doi: 10.3389/fbioe.2020.00797

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Copyright © 2020 Kaur, Kapoor, Kaundal, Dutta and Thakur.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) Structural superposition of Mtb RNAP β1 (marine)/CARD-RID (magenta) [PDB ID 4KBM] with Tth RNAP β1 (orange)/TRCF-RID complex (cyan) [PDB ID 3MLQ] shows the solvent-exposed conserved protein-protein interface. (B) Structural and sequence alignment of Mtb CarD-RID (4KBM chain B) with Tth TRCF-RID (3MLQ chain E). Mtb CarD-RID with Tth TRCF-RID do not share significant sequence similarity but do share the same site for interaction with RNAP β1 (shown in the rectangular box). The figure was generated using ESPript 3 server (Robert and Gouet, 2014). (C) Structural and sequence alignment of Mtb RNAP β1β2 (4KBM chain A) with Tth RNAP β1 suggests that both Mtb RNAP β1β2 and Tth RNAP β1 (3MLQ chain A) share the conserved site for interaction with transcription factor-RID (shown in the rectangular box). The figure was generated using ESPript 3 server (Robert and Gouet, 2014).