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. Author manuscript; available in PMC: 2016 Apr 29.
Published in final edited form as: Nature. 2015 Oct 12;526(7575):723–727. doi: 10.1038/nature15375

Figure 2.

Figure 2

Interactions among the domains in the ScACC holoenzyme. (a). The BT domain contacts the BC domain dimer. Side chains of residues in the interfaces between the BT domain (orange) and the BC domain of the same protomer (red) and the BC domain of the other protomer (salmon) are shown as stick models. (b). Interactions between the hook of the BT domain (orange) and the helical hairpin insert of AC1 domain (α8 and α9, green) and the β4A–β4B loop from the C domain of CT (yellow). (c). Interactions between domains AC1 (green) and AC2 (light green) of one protomer with the BC domain (salmon) of the other protomer.