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. 2015 May 7;290(26):16393–16402. doi: 10.1074/jbc.M115.641340

FIGURE 5.

FIGURE 5.

The Cα-Cα distance change measured upon c-di-AMP binding. The Cα-Cα distances of binding site residues (A) Asp-167, (B) Arg-169, and (C) Ile-164 are shown. The residue numbers in parentheses indicate the corresponding residue in B. subtilis KtrA. Upon c-di-AMP binding, the Cα-Cα distance between the residues dramatically decreased, indicating the tightening of the two KtrA RCK_C domain monomers.