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).
]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).