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Figure 1
(a) Asymmetric unit of ToxT (PDB entry 4mlo) colored by secondary structure. The N- and C-terminal residues (Lys5 and Gly272) of the model are indicated along with the disordered region between Asn132 and Phe134. The 310-helix spanning Leu99–Asp101 is colored blue. The PAM molecule and chloride ions are shown as cylinders and gold spheres, respectively. (b) Fo − Fc OMIT map contoured at 3σ (green mesh) for PAM and associated hydrogen bonds (dashed lines) to ToxT residues. (c) Enlarged view of the region from Ser87 to Glu110. Helix α1 spans Ser87–Ile98 and contains a kink at Leu94. This is followed by a 310-helix spanning Leu99–Asp101 and a shorter helix from Leu102 to Leu107 referred to as α1′.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 72| Part 9| September 2016| Pages 726-731
doi:10.1107/S2053230X1601298X
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