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. 2017 Mar 20;114(14):3726–3731. doi: 10.1073/pnas.1617868114

Fig. S10.

Fig. S10.

The 3D structure of E. faecalis RelQ and alignment with the ppGpp synthesis domain of E. coli RelA. (A) Secondary structure elements (α-helixes and β-sheets) of B. subtilis SAS1 (9) are indicated as spirals and arrows, respectively. Insertions in RelQ are highlighted in green, deletions are highlighted in red, and the C-terminal helix α5 is in yellow. Amino acid D82 (EF2671 locus numbering) is indicated with an orange asterisk. The first 17 characters are unaligned. The figure was generated using ESPript (34). (B) A homology model of the RelQ monomer based on B. subtilis SAS1 (18). Green indicates insertions, and red indicates the boundary of the deletion relative to RelA. Catalytically important amino acid D82 (EF2671 locus numbering) is highlighted in orange.