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. Author manuscript; available in PMC: 2013 Mar 7.
Published in final edited form as: Structure. 2012 Mar 7;20(3):479–486. doi: 10.1016/j.str.2012.01.009

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