Table 2.

Correlation of ToxA Mutations with Structure^a

Mutation	Structural Location	Accessible Side Chain Area (Å2)	Reference
Active
S86G	α1	60	This studyb
G96A	β2	11	Meinhardt et al. (2002)
T115A	β5	32	Manning et al. (2004)
T123A	β4-β5 loop	65	Manning et al. (2004)
T126A	β4-β5 loop	61	Manning et al. (2004)
V138A	β5-β6 loop	124	Manning et al. (2004)
T167A	β7-β8 loop	15	Manning et al. (2004)
G168A	β7-β8 loop	34	Manning et al. (2004)
Impairedc
Structurally disruptive
G93A	β2	25	This studyb
T132A	β5	3	Manning et al. (2004)
F147A	β6	33	Manning et al. (2004)
Structurally nondisruptive
G62A	N terminus loop	26	This studyb
C64G	N terminus loop	15	Tuori et al. (2000)
N136A	β5	73	Manning et al. (2004)
T137A	β5	45	Tuori et al. (2000)
T139A	β5-β6 loop	92	Manning et al. (2004)
R140A	β5-β6 loop	137	Manning et al. (2004)
G141A	β5-β6 loop	21	Meinhardt et al. (2002); Manning et al. (2004)
D142E	β6	83	Meinhardt et al. (2002); Manning et al. (2004)
V143A	β6	25	Manning et al. (2004)
Y144A	β6	109	Manning et al. (2004)
E145A	β6	91	Manning et al. (2004)
L146A	β6	66	Manning et al. (2004)

^aAll reported mutants were created and tested in the context of proToxA and behaved well during expression and purification.

^bResidues Gly62 and Gly93 are potential myristoylation sites; S86G was a PCR-induced mutation.

^cT132A and L146A are partially active; all other mutants in this category were scored as inactive.