Figure 4.
Figure 4 (A) Stereo view of the overlaid C[ ]-carbon
structures of CPD-2 (CP subdomain only; yellow sticks), CPA
(green sticks) and CPT (magenta sticks). The zinc ion (violet
sphere) belongs to the CPD-2 structure. Selected CPD-2 residues
are labelled. (B) View facing the funnel surrounding the active
site cleft superimposed with its solid Connolly surface
displaying the electrostatic potential [ranging from -15 k[B]T/e
(red) to +15 k[B]T/e (blue)] of CPD-2 (left), CPA (centre) and
CPT (right). The modelled substrate (CPD-2) and the coordinates
(PDB access code 6cpa) of a phosphonate inhibitor (CPA and CPT)
are also displayed, respectively, to highlight the active site.
(C) Stereo view of the C[ ]-carbon
structures of CPD-2 (CP subdomain only; yellow sticks) and CPA
(green sticks) in its complex with potato carboxypeptidase
inhibitor (blue sticks) (PDB access code 4cpa). Steric hindrance
prevents the latter from binding the regulatory CP. The zinc ion
(violet sphere) belongs to the CPD-2 structure. Some CPD-2
residues are labelled.
The above figure is reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1999,
18,
5817-5826)
copyright 1999.
]-carbon
structures of CPD-2 (CP subdomain only; yellow sticks), CPA
(green sticks) and CPT (magenta sticks). The zinc ion (violet
sphere) belongs to the CPD-2 structure. Selected CPD-2 residues
are labelled. (B) View facing the funnel surrounding the active
site cleft superimposed with its solid Connolly surface
displaying the electrostatic potential [ranging from -15 k[B]T/e
(red) to +15 k[B]T/e (blue)] of CPD-2 (left), CPA (centre) and
CPT (right). The modelled substrate (CPD-2) and the coordinates
(PDB access code 6cpa) of a phosphonate inhibitor (CPA and CPT)
are also displayed, respectively, to highlight the active site.
(C) Stereo view of the C[