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. 2021 May 11;12:2702. doi: 10.1038/s41467-021-22990-8

Fig. 6. σ70 NCR adopts a different conformation and interacts with β' clamp during promoter escape.

Fig. 6

a Superimposition of RDe1 with EcmrR-RPitc-4nt structures illustrates the large conformational changes of σ70 NCR and σ2 domain. The EcmrR NTD that is proximal to σ70 NCR is colored in yellow. b A close-up view of the σ70 NCR and β' clamp-toe interface superimposed with the cryo-EM density (blue surface) contoured at 5.5 σ. c Electrostatic surfaces of σ70 NCR and β' clamp-toe. The unit of electrostatic potential is kT/e. d Interactions between σ70 NCR and β' clamp-toe. Hydrogen bonds and salt bridges are shown as gray dotted lines. e Superimposition of σ70 NCR (bright colors) together with σ2 domain (pale colors) in RDe1 with those in EcmrR-RPitc-4nt, showing that σ2 domain stays largely static relative to σ70 NCR in the two structures. f Comparison of the σ2-β' clamp coiled-coil interactions between the structures of EcmrR-RPitc-4nt and RDe1. Hydrogen bonds and salt bridges are shown as yellow dotted lines. The surface areas buried between β' clamp coiled-coil and σ2 in the two structures are indicated.