Figure 3.
Figure 3. Modeling of the E1/PDHK complex. (a) The overall
stereo view of the E1 α-subunit with the modeled α-helical
substrate peptide (yellow) docked into the SC of the L2-free
PDHK subunit. The E1 β-chain and PDHK L2-bound subunit are
located far from the modeled interface and are omitted from the
model for clarity. (b) The close-up stereo view of the interface
between the E1 substrate α-helix (yellow) and the SC.
Hydrophobic side-chains of the substrate are shown in yellow,
the phosphorylation site (Ser264) that is modeled in close
proximity ( vert,
similar 3.3 Å) to the ATP (green) γ-phosphate is colored
in orange. The PDHK backbone and hydrophobic side-chains are
shown in the domain-dependent colors corresponding to those in
(a). The view is roughly the same as in Figure 1(b). (c)
Schematic drawing of the putative van der Waals interactions
(broken lines) that may be formed between the E1 substrate
α-helix and the PDHK hydrophobic residues in the SC. The color
scheme is the same as in (a) and (b).
The above figure is reprinted
by permission from Elsevier:
J Mol Biol
(2007,
370,
407-416)
copyright 2007.
vert,
similar 3.3 Å) to the ATP (green) γ-phosphate is colored
in orange. The PDHK backbone and hydrophobic side-chains are
shown in the domain-dependent colors corresponding to those in
(a). The view is roughly the same as in Figure 1(b). (c)
Schematic drawing of the putative van der Waals interactions
(broken lines) that may be formed between the E1 substrate
α-helix and the PDHK hydrophobic residues in the SC. The color
scheme is the same as in (a) and (b).