Figure 1.
Figure 1. Overall view of ApIDH dimer. Chains A and B are
colored red and green, respectively. The three domains are
indicated. The cysteine residues that form the disulfide bonds
are shown as a ball-and-stick model.
Figure 2.
Figure 2. Comparison of the monomer structures of (a) ApIDH,
(b) BsIDH and (c) EcIDH. Helices and strands are colored red and
yellow respectively. The serine residue targeted for
phophorylation of EcIDH (Ser113) and the corresponding residues
of other IDHs are represented by black spheres.
The above figures are
reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2004,
55,
1087-1089)
copyright 2004.