Figure 2.
Fig. 2. The mechanisms of domain movement. The -helix 1
(Ile^17-Arg25) and the loop region (Ala^26-Ile^37) of the C3-PLP
or C4-PLP complex in the open form (these residues are colored
pink and the others gray) change to the closed form on binding
of C5-PLP or C6-PLP (colored green). Ile^17 and Ile^37 are
anchored at the active site by hydrophobic interactions with the
substrate. Leu18 is located at the N-terminal end of -helix 1
and pulls the helix into the active pocket to shield the active
site from the solvent. This tugging of residues from Ile^17 to
Ile^37 changes the enzyme from the open to the closed form.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2000,
275,
18939-18945)
copyright 2000.
-helix 1
(Ile^17-Arg25) and the loop region (Ala^26-Ile^37) of the C3-PLP
or C4-PLP complex in the open form (these residues are colored
pink and the others gray) change to the closed form on binding
of C5-PLP or C6-PLP (colored green). Ile^17 and Ile^37 are
anchored at the active site by hydrophobic interactions with the
substrate. Leu18 is located at the N-terminal end of