TABLE 3.
Binding affinity data for tested FliI, HrcN, and ClpB2 variants
Dissociation constant (KD) values for the ATPase proteins analyzed in this study are shown. Binding to FliISeT was concentration-dependent but did not saturate in the kinetic experiment.
| KD | |
|---|---|
| μm | |
| FliIHis (full-length) | 2.4 ± 0.2 |
| FliIΔ1–18 (N-terminally truncated) | 0.8 ± 0.03 |
| FliIΔ1–18 R170H | Not determined |
| FliIΔ1–18 E208Q | Not determined |
| FliIΔ1–18 R337H | Not determined |
| FliIPto (Pto DC3000) | 7.6 ± 0.8 |
| FliISeT (S. enterica) | Not determined |
| FliISm (S. meliloti) | 3.2 ± 0.7 |
| HrcNHis | 3.2 ± 0.2 |
| ClpB2His | 9.5 ± 0.5 |
| FliI G176A (Walker A mutant) | 11.0 ± 1.1 |
| FliI K181A (Walker A mutant) | 2.2 ± 0.2 |
| HrcN K181A (Walker A mutant) | 3.8 ± 0.4 |
| FliI D265A (Walker B mutant) | 4.5 ± 0.2 |