Table 1.
Equilibrium dissociation constants (Kd) reported for solute binding proteins of Mn-specific ATP-binding cassette transporters and for human calprotectin.
| Protein | Method | Kd (Mn), nM | Kd (Zn), nM |
|---|---|---|---|
| Spn PsaA SBPa | ITC | 3.3 (±0.1) | 230 (±2) |
| Tpa TroA SBPb | ITC | 7.1 (±0.5) | 22 (±4) |
| Ype YfeA SBPc | ITC | 18 (±6) | 6.7 (±1.6) |
| Ssu TroA SBPd | ITC | 250 (±20) | 430 (±10) |
| Sau MntC SBPe | ITC, competition | 3.8 (±1.1) | not determined |
| Calprotectin + Ca(II)f,g | chelator comp | 190; 21000 | <0.01; <0.24 |
| Calprotectin + Ca(II)h | ITC | 1.3; 3700 | 1.4; 5.5 |
20 mM NaH2PO4, pH 6.5, 25 °C, 4.5–20 μM PsaA (McDevitt et al., 2011).
100 mM sodium acetate, pH 6.5, 20 °C, 40 μM TroA (Desrosiers et al., 2007).
100 mM sodium acetate, pH 6.5, 20 °C, 42 μM YfeA (Desrosiers et al., 2010).
20 mM sodium acetate, pH 6.5 at 25 °C, 30 or 90 μM TroA (Zheng et al., 2011).
50 mM citrate, 150 mM NaCl, 10% glycerol, pH 6.0, 25 °C, 36–43 μM MntC (Gribenko et al., 2013).
Mn parameters measured in 75 mM Hepes, 100 mM NaCl, 0.2 mM Ca(II), pH 7.5, 25 °C. Values for metal site 1 (S1; His6) and metal site 2 (S2; His3Asp) are shown as KdMn1, KdMn2, KdZn1, and KdZn2 (Figure 5).
Zn parameters measured in 75 mM Hepes, 100 mM NaCl, 1 mM Ca(II), pH 7.5, room temperature.