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. 2020 Sep 30;295(50):16960–16974. doi: 10.1074/jbc.RA120.014083

Figure 7.

Figure 7.

Schematic representation of proposed mechanism. Hydrophobic packing of trans-acting Tyr290 with cis-acting Arg349 is pivotal in maintaining the heptameric state, which is required for ATPase activity. In the presence of c-di-GMP, FlrC loses heptameric state with abrogation of ATPase activity.