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. Author manuscript; available in PMC: 2007 Dec 3.
Published in final edited form as: Structure. 2007 Jul;15(7):793–805. doi: 10.1016/j.str.2007.05.009

Figure 7.

Figure 7

Human and B. stearothermophilus TrpRSs use distinct mechanism to close the active site for catalysis. (A) In B. stearothermophilus TrpRS, ligand binding induces a 13° ‘hinge-like’ motion— between the Rossmann fold domain and the anticodon recognition domain—to close the ATP binding cleft. (B) Human TrpRS stays in a conformation similar to the ‘closed’ conformation of B. stearothermophilus TrpRS. Ligand binding engages the β1-β2 hairpin (from the eukaryote-specific patch) to cap the active site.