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Figure 6.
Figure 6. Comparison of the tertiary structure of EF-1β and
the GEF domain of EF-Ts. (a) Side-by-side ribbon diagrams of the
GEF domain of E. coli EF-Ts (residues 57–139) and
hEF-1β[135–224]. The structure on the left is the GEF-domain
of EF-Ts (α helices in red and yellow, β sheet in cyan) from
the complex with EF-Tu [20] . The sPhe81 sidechain is shown in
dark blue. The mean structure of hEF-1β[135–224] (α helices
in green and yellow, β sheet in dark blue) is shown on the
right, with the loop between β2 and β3 in magenta and
the sidechain of Tyr181 in yellow. (b) Superposition of the GEF
domain of EF-Ts and hEF-1β[135–224]. The color scheme is
identical to that in (a). Nineteen Cα atoms from each structure
were chosen for a least-squares superposition. This figure was
prepared using the program MOLMOL [54] .
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