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. Author manuscript; available in PMC: 2015 Sep 11.
Published in final edited form as: Cell. 2014 Sep 11;158(6):1389–1401. doi: 10.1016/j.cell.2014.07.046

Figure 5. Large conformational differences in the structure of apo LmPC.

Figure 5

(A). Overlay of the structure of LmPC in complex with c-di-AMP (in color) with that of apo LmPC (in gray). The superposition was based on monomer 1. Large differences in the positions of the other monomers are visible. (B). Conformational differences in the c-di-AMP binding site in the structure of apo LmPC. (C). Molecular surface of apo LmPC at the CT dimer interface. The c-di-AMP molecule would clash with the enzyme in this conformation. (D). Overlay of the four monomers of the LmPC tetramer in the complex with c-di-AMP. The superposition is based on the CT domain only. A small conformational difference is seen for the BC domain. (E). Overlay of the four monomers of the apo LmPC tetramer. Large differences are observed in the positions and orientations of the BC domains.