Figure 2.
Figure 2 The structure of the polymerase:terminal protein
heterodimer. (A) A ribbon representation, with polymerase
colored according to Kamtekar et al, 2004, and terminal protein
shown with cylindrical helices. (B) A view of the complex
rotated 90° from that shown in (A), with terminal protein
shown as cylinders underneath a transparent surface. (C) A C[
]trace
of polymerase from the polymerase:terminal protein complex (in
color) superimposed on the apo polymerase structure. Significant
differences in conformation occur only in a loop between
residues 304 and 314 (shown in magenta in the complex and in
black in the apo polymerase structure). The polymerase active
site is marked by the space-filling representations of the
carboxylates that coordinate the catalytic metal ions. (D)
Terminal protein in the same orientation as in (B).
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
EMBO J
(2006,
25,
1335-1343)
copyright 2006.
]trace
of polymerase from the polymerase:terminal protein complex (in
color) superimposed on the apo polymerase structure. Significant
differences in conformation occur only in a loop between
residues 304 and 314 (shown in magenta in the complex and in
black in the apo polymerase structure). The polymerase active
site is marked by the space-filling representations of the
carboxylates that coordinate the catalytic metal ions. (D)
Terminal protein in the same orientation as in (B).