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. Author manuscript; available in PMC: 2014 Nov 5.
Published in final edited form as: Structure. 2013 Oct 3;21(11):10.1016/j.str.2013.08.021. doi: 10.1016/j.str.2013.08.021

Figure 2. Ser-SA induced conformational change in human SerRS is caused by shifting the TBD-AD interactions from α13 in lower organisms to α9–α10 in human SerRS (see also Figure S5).

Figure 2

The hydrogen bonding interactions in the “hinge” region mediating TBD (yellow) and AD (green) in crystal structures of (A) human SerRS bound with Ser-SA (PDB 4L87) (B) ligand-free human SerRS (PDB 3VBB) (C) C. albicans SerRS bound with Ser-SA (PDB 3QO8) (D) T. brucei SerRS bound with ATP (PDB 3LSS) (E) P. horikoshii SerRS bound with Ser-SA (PDB 2DQ0) and (F) T. thermophiles SerRS bound with Ser-SA (PDB 1SET). The secondary structures are labeled in gray.