Fig. 6: HelD release and RNAP-HelD complex dimerization.
From: The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling
a Close-up view of the ATP-binding site of HelD, with ADP-Mg2F3 from a UvrD complex (PDB ID 2IS6) transferred by superpositioning of the UvrD NTPase domains on HelD, illustrating clashes with the nucleotide. ADP-Mg2F3 shown as sticks and colored by atom type; carbon, beige; nitrogen, blue, oxygen, red, phosphorus, orange; magnesium ions, green; fluoride ions, light blue. b SDS-PAGE analysis of SEC runs after treating RNAP-δ-HelD with buffer or the nucleotides indicated on the left. Experiments were repeated independently at least twice with similar results. For full gels, see Supplementary Fig. 7b. c Structure of dimeric RNAP-δ-HelD. Inset, close-up view on the dimer interface. The two protomers interact via the elements highlighted in colors; β′ clamp, violet; C-terminal β clamp, green; β flap tip (FT), olive; residue 811–821 of the β flap (Flap811–821), yellow. d Structure of a hibernating RNAP I dimer (PDB ID 4C2M). A135 subunit, black; A190 subunit, white; small subunits, beige. Inset, close-up view on the dimer interface. A190 clamp, violet; C-terminal A135 clamp, green.
