Table 2. Binding of monomeric VLR4 to recombinant BclA-CTD variants.
VLR4 has similar binding affinities for BclA despite amino-acid changes corresponding to differences in the sequences of BclA of B. anthracis Sterne, B. cereus T and B. thruingiensis Kurstaki. The BclA mutation created to disrupt crystal packing, Thr185Asn, shows a slight increase in affinity for VLR4. See also supplemental Figure S3.
| Sample | Kd (M) |
|---|---|
| BclA-CTD-B. anthracis Sterne | 2.6×10−6 |
| BclA-CTD-Thr185Asn | 0.6×10−6 |
| BclA-CTD-Ser129Ala | 3.2×10−6 |
| BclA-CTD-Glu130Gln | 2.4×10−6 |
| BclA-CTD-Pro159Ser | 3.5×10−6 |
| BclA-CTD-Ser129Ala-Pro159Ser | 4.2×10−6 |
| BclA-CTD-Glu130Gln-Pro159Ser | 3.2×10−6 |
| BclA-CTD-B. cereus T | 3.5×10−6 |
| BclA-CTD-B. thruingiensis Kurstaki | 3.4×10−6 |