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. 2021 Aug 3;12:4690. doi: 10.1038/s41467-021-25029-0

Fig. 4. Comparison of conformational states of β-subunits.

Fig. 4

Superposition (on the N-terminal β-barrel) of the four main conformational states seen in the TF1(βE190D) (this study; β0HCTP, β200CTP*, β240HODPP, and β320ODP), and the half-open state observed for bMF120 (pdb1h8e). β200CTP* (black) is in a fully closed state, β320ODP (red) is in a fully open state, β0HCTP and β240HODPP are intermediate structures that are either half closing or half opening, and β320HC1h8e is an intermediate structure of bMF1 similar to the open conformation. a Individual unique conformations compared to one other and viewed from the side. b Unique conformations superimposed and viewed from below.