|
Figure 3.
Figure 3. The R1E protein. (a) The R1E dimer structure. The
N-terminal domains are coloured in blue-green, the small domains
in gold. The catalytic ten-stranded α/β barrel is coloured
brown in one monomer and beige in the other. One hydrophobic
cleft of R1E is marked (blue peptide) as well as the helices
forming the cleft. The radical forming C388 at the active sites
are marked as spheres coloured by atom. The dGTP effectors on
each side of the dimer interface are shown in sticks. Three
loops are marked. Flexible parts of the loops are indicated by
broken lines. (b)The effector dGTP at the specificity site of
R1E. In brown is the initial F[o]−F[c] electron density map
contoured at 3.0σ and in light grey the final 2F[o]−F[c]
density map contoured at 1.0σ. The loop shown in the picture,
loop 1, is stabilised by the binding of the effector. The
magnesium ion is colored magenta with the F[o]−F[c] omit map
for the Mg in green (contoured at 3.0σ). Figure 3. The R1E
protein. (a) The R1E dimer structure. The N-terminal domains are
coloured in blue-green, the small domains in gold. The catalytic
ten-stranded α/β barrel is coloured brown in one monomer and
beige in the other. One hydrophobic cleft of R1E is marked (blue
peptide) as well as the helices forming the cleft. The radical
forming C388 at the active sites are marked as spheres coloured
by atom. The dGTP effectors on each side of the dimer interface
are shown in sticks. Three loops are marked. Flexible parts of
the loops are indicated by broken lines. (b)The effector dGTP at
the specificity site of R1E. In brown is the initial F[o]−F[c]
electron density map contoured at 3.0σ and in light grey the
final 2F[o]−F[c] density map contoured at 1.0σ. The loop
shown in the picture, loop 1, is stabilised by the binding of
the effector. The magnesium ion is colored magenta with the
F[o]−F[c] omit map for the Mg in green (contoured at 3.0σ).
|
