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. Author manuscript; available in PMC: 2013 Jul 1.
Published in final edited form as: Mol Cell. 2012 Jun 14;46(6):735–745. doi: 10.1016/j.molcel.2012.05.029

Figure 4. Recognition of c-di-GMP by STING.

Figure 4

(A) Difference Fourier (Fo-Fc) map contoured at 2.5 σ at the dimer interface, superimposed with the bound c-di-GMP.

(B) Cartoon representation of STING/c-di-GMP complex. One STING molecule is colored in violet and the other in wheat. The c-di-GMP molecule is shown as a stick model.

(C) Superposition of the STING/c-di-GMP complex with the free STING dimer. The STING protomers in the complex are colored in violet and wheat, while those in the free STING are in green and gray. Red arrow marks the slight outward swing of the STING molecule (wheat) in the complex with c-di-GMP.

(D) Isothermal titration calorimetry measurement for the interaction between STING and c-di-GMP.

(E) Stick representation of c-di-GMP with the intrinsic two-fold symmetry. The orientation is the same as in (C). 2-position nitrogen of the guanine ring, 2′-hydroxyl group of the ribose, and the phosphoryl oxygen atoms are labeled.

(F) Detailed interaction of c-di-GMP with STING. For clarity, only one “half site” is shown. Contacting residues are labeled, and hydrogen bonds are represented by dotted lines.