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. 2015 Jul 16;290(36):22225–22235. doi: 10.1074/jbc.M115.669267

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© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

Author's Choice—Final version free via Creative Commons CC-BY license.

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FIGURE 5. — The influence of CAP-cAMP contacts on changes to allostery induced by second site mutations. The charts show the change in allosteric cooperativity induced by mutations in ENM^WT (ΔK₂/K₁ ENM^WT) subtracted from the change in allosteric cooperativity induced by the same mutation in ENM^G71/E72 (ΔK₂/K₁ ENM^G71/E72) (a), ENM^R82/S83 (ΔK₂/K₁ ENM^R82/S83) (b), or ENM^T127/S128 (ΔK₂/K₁ ENM^T127/S128) (c) plotted against amino acid number in CAP. The colored backgrounds indicate the cAMP-binding domain (pale blue), interface forming α helix (white), and DNA-binding domain (red).