Figure 5.
Figure 5: Hypothetical model of the receptor-bound,
membrane-inserted PA pore. The model is based on the pre-pore
PA[63] crystal structure^6, channel conductance studies8, and
the crystal structure of -haemolysin19.
The barrel is formed by rearrangement in each monomer of the
segment shown in red in Fig. 3. Each PA[63] monomer is shown in
a different colour. Residues 303 -324 form the membrane-spanning
region of the barrel. Seven copies of the CMG2 I domain bound to
the heptamer are in blue. The 40
Å gap between the CMG2 I domain and the membrane may be occupied
by a 100-residue
domain of CMG2, C-terminal to the I domain, which precedes its
membrane-spanning sequence.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2004,
430,
905-908)
copyright 2004.
-haemolysin19.
The barrel is formed by rearrangement in each monomer of the
segment shown in red in Fig. 3. Each PA[63] monomer is shown in
a different colour. Residues 303 -324 form the membrane-spanning
region of the barrel. Seven copies of the CMG2 I domain bound to
the heptamer are in blue. The 
40
Å gap between the CMG2 I domain and the membrane may be occupied
by a