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. 2022 Jan 21;13:432. doi: 10.1038/s41467-022-28078-1

Fig. 2. Structure of MtbEttA and its interaction with the Mtb 70SIC in the Pre_R0 state.

Fig. 2

a The structure and domain composition of MtbEttA. Nucleotide-binding domains 1 (NBD1, residues 2-93 and 137-240) and 2 (NBD2, residues 308-545), arm domain (residues 94-136), P-tRNA interacting motif (PtIM, residues 239-307), and the C-terminal basic tail (residues 550-557) are colored in thistle, light steel blue, medium purple, violet, and indigo, respectively. Nucleotide-binding sites (NBS-I and NBS-II) are indicated by arrows. b The overall interactions between MtbEttA and surrounding RNAs and proteins. The relative location of the peptidyl transferase center (PTC) is outlined by a dashed oval. Structural details of boxed regions are described in panels (cf). c The C-terminal tail is inserted between the L1 stalk and NBD1. d PtIM α1 is in close contact with Helix 68 of 23S rRNA. e The tip of PtIM reaches towards the PTC, and interacts with the CCA tail of the P-site tRNA, Helices 74, 75, and 93 of the 23S rRNA. f Interactions between MtbEttA and the 30S. A salt bridge is observed between E526 (MtbEttA) and R112 (uS7). Basic residues in MtbEttA (R316 and R346) point towards helices 41 and 42 of the 16S rRNA. Several rRNA nucleotides are labeled to show the regions of interactions.