Table 1 Biolayer interferometry data on dUTPase:Stl complexes (Curves and fitting is displayed on Figures S2-S8 in the Supporting information).

From: Antirepressor specificity is shaped by highly efficient dimerization of the staphylococcal pathogenicity island regulating repressors: Stl repressor dimerization perturbed by dUTPases

sensor

analyte

KD (nM)*

ka (M−1 s−1)*

kdis (s−1)*

χ2#

hDUT

Sa-Stl

9.75

6.7·104

6.5·10–4

3.07

Sa-Stl

hDUT

0.18

1.5·106

2.7·10–4

1.20

Sho-Stl

hDUT

4.54

5.2·104

2.3·10–4

0.57

Sho-Stl-NDY

hDUT

7.62

3.1·104

2.4·10–4

4.54

hDUT

Sho-Stl

Strongly distorted binding curves

Sho-Stl

mtDUT

0.013 ± 0.008§

2.2·104

2.9·10–7 ± 1.8§

0.12

mtDUT

Sho-Stl

35

1.2·104

4.1·10–4

0.48

  1. hDUT: human dUTPase; Sa-Stl: S. aureus SaPIbov1 Stl; Sho-Stl: S. hominis ShoCI794_SEPI Stl; Sho-Stl-NDY: K99N, E100D, F105Y triple mutant Sho-Stl, which has the same dUTPase binding motif as Sa-Stl, mtDUT: Mycobacterium tuberculosis dUTPase.
  2. *If not shown the error of fitted values was below 1%
  3. #χ2 < 5 statistics considered as a good fit.
  4. §Close to the detection limit.
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