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. Author manuscript; available in PMC: 2013 Jun 20.
Published in final edited form as: J Am Chem Soc. 2012 Jun 6;134(24):10286–10298. doi: 10.1021/ja303695u

Figure 2.

Figure 2

(A) Models from X-ray crystal structures of the unliganded open (cyan, PDB entry 5TIM) and PGH-liganded closed (green, PDB entry 1TRD) forms of TIM from Trypanosoma brucei brucei in the region of the enzyme active site. Closure of loop 6 (residues 168 – 178, Scheme 2) over the bound phosphodianion ligand results in movement of the hydrophobic side chain of Ile-172 toward the carboxylate side chain of the catalytic base Glu-167. This is accompanied by movement of Glu-167 toward the hydrophobic side chain of Leu-232, that maintains a nearly fixed position. (B) A structure that shows the positions of Ile-172 and Leu-232 at the active site “hydrophobic cage” for wildtype Trypanosoma brucei TIM in complex with PGH (PDB entry 1TRD).