Figure 2.
Figure 2 Structure of the Mt ClpP1 monomer. (a) Ribbon-diagram
representation, with labelling of the secondary-structure
elements according to the structure of Ec ClpP1 (Wang et al.,
1997[Wang, J., Hartling, J. A. & Flanagan, J. M. (1997). Cell,
91, 447-456.]). The chain is coloured from blue to red from the
N-terminus to the C-terminus. The catalytic triad (Ser98, His123
and Asp172) is shown in stick representation. (b) A comparison
of the C^ backbone
of ClpP monomers corresponding to Mt (blue), Sp (green), Ec
(gold), Pf (violet) and Hs (red). Amino acids from the head
domains (residues 28-124 and 160-190 in Mt ClpP1) were selected
for superimposition. (c) A 90°-rotated view from (b) showing
a significant shift of the E
helix in the handle domain of the Mt ClpP1 monomer.
The above figure is reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2007,
63,
249-259)
copyright 2007.
backbone
of ClpP monomers corresponding to Mt (blue), Sp (green), Ec
(gold), Pf (violet) and Hs (red). Amino acids from the head
domains (residues 28-124 and 160-190 in Mt ClpP1) were selected
for superimposition. (c) A 90°-rotated view from (b) showing
a significant shift of the