Figure 3 - full size

Figure 3. Fig. 3. Crystal structure of [2] subunit alone of tryptophan synthase from P. furiosus. (A) The overall structure of the tryptophan synthase [2] dimer from P. furiosus. The N-terminal (1–200) and the C-terminal (201–388) residues are coloured red and blue, respectively. Arrows point to the first two strands and one helical structure (residue 58–64) that intrude into the C domain. The PLP molecule is represented as a CPK model, coloured gold. Drawings were prepared using MOLSCRIPT[71]. (B) Two similar N and C domains of Pf were superimposed using 69 C pairs fitted well among the 73 residues of St , which are reported to deviate by less than 4.0 Å between both domains [3]. The N and C domains are depicted in gold and green, respectively. Fitting used program LSQKAB[72].

The above figure is reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2004, 271, 2624-2635) copyright 2004.