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. Author manuscript; available in PMC: 2012 Mar 29.
Published in final edited form as: Nature. 2011 Sep 4;477(7366):616–620. doi: 10.1038/nature10404

Figure 3. T. curvata PARG crystal structure in complex with ADP-ribose.

Figure 3

a, b, Overall fold of PARG with α-helices depicted in red, β-sheets in blue and bound ADP-ribose in green spheres. The PARG-specific catalytic loop is shown in yellow, and the diphosphate-binding loop in magenta. c, Overlay of the T. curvata PARG structure with a representative macro domain structure (PDB code 2BFQ, in cyan). The PARG-specific N-terminal extension and additional PARG structural elements are highlighted in red. Structural features that are similar to 2BFQ and other macro domains are shown in gray. d, Detailed view of ADP-ribose bound in the PARG active site. ADP-ribose is shown with the corresponding 2Fo-Fc omit-map density contoured at 1.2 σ in blue. Key active site residues are represented in atom coloured sticks with hydrogen bonds indicated by black dotted lines.