|
Figure 6.
Figure 6. The interaction between CcdB and GyrA. (a)
Structure of the 59 kDa N-terminal domain of GyrA (GyrA59). The
T-gate domain, which forms the primary dimer interface, is
coloured green, the CAP-like domain red, the tower domain blue,
and the connecting helices grey. Arg462 is shown as a dark grey
CPK model. The position of Gly214 is indicated by a large sphere
around the position of its C^aatom. In this conformation, both
the G-gate and the T-gate are closed and the central hole is not
large enough to accommodate a CcdB dimer in any orientation. (b)
CcdB docked to GyrA59 in the open G-gate conformation, where the
head dimer interface is disrupted. The GyrA59 dimer is shown in
the same colours as in (a), and the CcdB dimer is shown in cyan.
Ample space is present for CcdB binding and CcdB can be rotated
around the 2-fold axis of the complex to increase the contact
area without inducing severe steric clashes.
|
