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. Author manuscript; available in PMC: 2016 Apr 23.
Published in final edited form as: Cell. 2015 Apr 9;161(3):501–512. doi: 10.1016/j.cell.2015.03.040

Figure 5. ATPase1 is held in an autoinhibited state by inter-ATPase interactions.

Figure 5

(A) Crystal structure of TcEccC(cyto) with inset highlighting the interface between ATPase1 and ATPase2. (B) Logo diagram representing the alignment of 142 unique EccC sequences. (C) Disruption of ATPase1-ATPase2 interface by R543A mutation activates the ATPase activity of TcEccC, which requires the Walker B catalytic residue in ATPase1 (E593Q). An analogous mutation between ATPase2 and ATPase3, R892A, led to a small increase in activity. The graph represents three measurements of ATPase activity at an enzyme concentration of 1 μM ATPase with saturating ATP*MgCl2 (10 mM). Also see Figure S4.