Figure 8.
Figure 8 (A) Highest score docking model of the Trbp111–tRNA
complex showing surface complementarity and tRNA binding mode.
The protein dimer is shown in a Connolly surface representation
(generated in the program InsightII; Molecular Simulations, San
Diego, CA) of all non-hydrogen atoms, superimposed on a C[ ]trace.
The monomers are shown in different colors. tRNA is shown as
sticks. The asterisk denotes the observed cleft (putative
tRNA-binding site). Loop L6 is also labeled. (B) Side view of
(A) looking down the tRNA acceptor stem helix. The surface
electrostatic potential on the Trbp111 dimer is shown. Positive
charge potential is shown in blue and negative charge potential
in red. The surface is superimposed on a ribbon diagram of the
protein. The tRNA is shown in green as a ribbon through the
backbone phosphate groups.
]trace.
The monomers are shown in different colors. tRNA is shown as
sticks. The asterisk denotes the observed cleft (putative
tRNA-binding site). Loop L6 is also labeled. (B) Side view of
(A) looking down the tRNA acceptor stem helix. The surface
electrostatic potential on the Trbp111 dimer is shown. Positive
charge potential is shown in blue and negative charge potential
in red. The surface is superimposed on a ribbon diagram of the
protein. The tRNA is shown in green as a ribbon through the
backbone phosphate groups.