Figure 2.
Figure 2. Comparison of Mouse and human DcpS. (A) Ribbon
diagram of the Mouse DcpS dimer. Chain A is in gray and chain B
is in pink. The dimer is symmetric with a C -C
distance
between Asp110 and Trp174 of 28
Å. Residues 131 and 147 flanking the linker region are
labeled. (B) Ribbon diagram of the human DcpS/mGpppG complex.
Chain A is shown in gray and chain B in purple. The dimer has a
symmetric bottom and an asymmetric top and features an open side
and a closed side with a 36 Å and 6 Å C -C
gap
between Asp111 and Trp175, respectively. The mGpppG nucleotides
bound to the active sites are shown in ball-and-stick
configuration, with carbon atoms colored in yellow, phosphorous
in purple, oxygen in red, and nitrogen in blue. The movement of
the N-terminal domain is facilitated by a conformational change
in the linker region around helix 3.
Superposition of the DcpS active sites in the relaxed empty
state with the open (C) and closed (D) mGpppG bound state. The
mGpppG-interacting residues from human DcpS (gray, residues
labeled in brackets) and their counterparts in Mouse DcpS (blue)
are shown in ball-and-stick configuration.
-C
28
Å. Residues 131 and 147 flanking the linker region are
labeled. (B) Ribbon diagram of the human DcpS/mGpppG complex.
Chain A is shown in gray and chain B in purple. The dimer has a
symmetric bottom and an asymmetric top and features an open side
and a closed side with a 36 Å and 6 Å C 
3.
Superposition of the DcpS active sites in the relaxed empty
state with the open (C) and closed (D) mGpppG bound state. The
mGpppG-interacting residues from human DcpS (gray, residues
labeled in brackets) and their counterparts in Mouse DcpS (blue)
are shown in ball-and-stick configuration.