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. 2017 Jun 26;114(31):8211–8216. doi: 10.1073/pnas.1702741114

Fig. S1.

Fig. S1.

Structures of the T. thermophilus RNAP holoenzyme DNA complex mimicking the pyrG promoter open complex. (A) Ribbon models of RNAP domains and motifs are shown with transparent surfaces of the σ-factor and the β-flap domain (TL, trigger loop; BH, bridge helix). DNA strands are shown as stick models (template DNA, dark green; nontemplate DNA, light green). The disordered region of the TL is shown as a dashed line. The nucleotide binding sites (i and i+1) are indicated, and the active site catalytic Mg2+ is shown as a yellow sphere. The gray mesh shows the 2FoFc electron density for the DNA strands contoured at 1.5 σ. (B) Stick models of the downstream DNA and the β-subunit fork loop 2 are shown with their 2FoFc electron densities (gray mesh) contoured at 1.5 σ. Hydrogen bonds between DNA bases and the salt bridge between +3G and R422 are depicted as red dashed lines.