Supplementary Figure 5: KlDcp2-Edc3 interface.
From: Structure of the active form of Dcp1–Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator
A. Sequence alignment of the Sp, Sc and KlDcp2 region involved in Edc3 binding. Strictly conserved residues are in white on a black background. Partially conserved residues are boxed. Residues involved in Edc3 binding are indicated by black stars below the alignment.
B. Sequence alignment of Sp, Sc and KlEdc3 LSm domain. Strictly conserved residues are in white on a black background. Partially conserved residues are boxed. Residues involved in Dcp2 binding are indicated by black stars below the alignment. Panels A and B were generated using the ESPript server.
C. Detailed representation of KlDcp2-Edc3 interface. Some side chain residues from the interface are shown as sticks.
D. Superimposition of SpDcp2-Edc3 complex determined by NMR (SpDcp2 and SpEdc3 LSm are in yellow and grey, respectively) onto KlDcp2-Edc3 as observed in our structure. Some side chain residues from both Dcp2 proteins are shown as sticks.
E. Comparison of Edc3 LSm residues involved in Dcp2 binding. The superimposition shown in panel E is viewed from a different angle as panel D using the same color code. Some side chains from SpEdc3 and KlEdc3 involved in Dcp2 binding are shown as sticks.
