Skip to main content
. Author manuscript; available in PMC: 2015 Aug 28.
Published in final edited form as: Cell. 2014 Aug 14;158(5):1011–1021. doi: 10.1016/j.cell.2014.07.028

Figure 1. Structure of Vibrio cholerae DncV reveals an auto-activated cGAS-like enzyme.

Figure 1

(A) Crystal structure of Vibrio cholerae DncV. Alpha helices are colored in green, beta strands forming the enzyme core are in blue, and a red circle marks the active site. (B) Superposition of the crystal structures of DncV (green) and human cGAS (purple) (PDB 4KM5). (C) Surface view representation of the DncV (green), apo human cGAS (purple, “inactive”) and dsDNA-bound mouse cGAS (purple, “active”) active site substrate channels (Mouse cGAS PDB 4K98). Nucleotide substrate binding pockets are colored in blue and the active site is marked by a red circle. (D) Superposition of an electrostatic surface view of DncV colored by charge (positive, blue and negative, red) and cGAS-bound dsDNA (green). The structures of DncV and dsDNA-bound mouse cGAS were superposed without manual fitting of the dsDNA ligand. See also Figure S1.