Figure 2. Stereo views of the electron density (2F[o]–F[c]
at 1σ) showing the two conformers of Tyr10 in the G-site. (a)
R21L, showing Tyr^out10 at H-bond distance from Asp33. The new
residue, Leu21 is at a distance of 4 Å from Tyr10.
Tyr^out10 hinders the movement of the Arg35 side-chain, as
displayed in Figure 1(b). (b) GTX-bound wtGST, showing the polar
interaction between the hydroxyl group of the Tyr^in10 and the
sulphur atom of GTX. Tyr10, Arg21, Asp33 and Arg35 are
orientated as shown in Figure 1(a).
The above figure is reprinted
by permission from Elsevier:
J Mol Biol