Figure 1.
Fig. 1. Key structural features of wild-type Cu,Zn SOD. (a)
In the right-hand subunit (chain A), copper (orange) and zinc
(grey) are shown as spheres. Loop IV is divided into three
sections: the dimerization subloop (residues 50–54, yellow)
creates part of the dimer interface, the disulfide subloop
(residues 55–61, raspberry) covalently attaches to the
β-barrel via the Cys57–Cys146 disulfide, and the zinc-binding
region (residues 62–83, blue) contains His63, His71, His80,
and Asp83 (shown as sticks). Copper is coordinated by residues
His63, His46, His48, and His120 (orange sticks). (b) Surface
buried upon dimerization is shown for chain A. The vert,
similar 1400-Å^2 area is divided into three regions: the
area contributed by the dimerization subloop (yellow), the area
buried by the interaction with the dimerization subloop of chain
B (cyan with yellow ribbon showing chain B segment), and the
area from the β-barrel interaction (light grey). The
dimerization subloop is involved in vert,
similar 75% of the total surface area buried by the dimer.
The above figure is reprinted
from an Open Access publication published by Elsevier:
J Mol Biol
(2007,
373,
877-890)
copyright 2007.
vert,
similar 1400-Å^2 area is divided into three regions: the
area contributed by the dimerization subloop (yellow), the area
buried by the interaction with the dimerization subloop of chain
B (cyan with yellow ribbon showing chain B segment), and the
area from the β-barrel interaction (light grey). The
dimerization subloop is involved in