Figure 2 - full size

 

Figure 2.
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 (2006, 360, 678-689) copyright 2006.