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. 2010 Nov 11;6(11):e1000994. doi: 10.1371/journal.pcbi.1000994

Figure 1. Structure of the α/β–dimeric unit of tryptophan synthase.

Figure 1

(a) A labeled diagram of the α/β–dimeric unit of tryptophan synthase (TRPS). The important regions have been color coded: blue for α–L2 (residues α53–60), red for α–L6 (residues α179–193), purple+pink for the β–COMM domain (residues β102–189), and pink for the β–H6 of COMM domain (residues β165–181). The approximate location of the interconnecting channel is shown as a solid brown line. (b) The network of H–bonds at the α/β–interface of the TRPS dimeric unit. Some of the H–bonds play key roles in allosteric communications and the substrate channeling process. The interacting pair of residues is zoomed in, and the formation of possible H–bonds is shown in small panels.