Figure 1
Crystal structure of the KPR–2′P-ADP-ribose binary complex and comparison with the KPR–NADP+ complex. (a) 2′P-ADP-ribose electron density. The final 2Fo − Fc electron-density map for 2′P-ADP-ribose contoured at 1σ is shown in blue. Binding modes of (b) 2′P-ADP-ribose and (c) NADP+ and the key residues at the active site of KPR are shown. The van der Waals surface of the N-terminal domain (residues 1–176) only is shown, coloured by electrostatic potential (neutral, white; positive, blue; negative, red). (d) Superposition of the KPR–NADP+ (salmon pink) and KPR–2′P-ADP-ribose (yellow) structures. The protein structures were superposed using the backbone atoms of residues 2–291. |