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. Author manuscript; available in PMC: 2018 Sep 6.
Published in final edited form as: ACS Infect Dis. 2017 Mar 21;3(5):378–387. doi: 10.1021/acsinfecdis.7b00003

Figure 7.

Figure 7.

Further observed structural shift of α9 helix away from the active site, restructuring the connecting loop, and resulting in the loss of thermal stability. (a) Alignment of the Ag85C ebselen structure (gray; PDB, 4QDU) with the Ag85C azido ebselen structure (beige). (b) Alignment of the Ag85C ebselen structure (gray; PDB, 4QDU) with the Ag85C adamantyl ebselen structure (orange). (c) Overlay of α-helix 9 between native enzyme (green; PDB, 1DQZ), ebselen modified enzyme (gray; PDB, 4QDU), azido ebselen modified enzyme (beige), and adamantyl ebselen modified enzyme. (d) Ag85C modified with ebselen or either of the derivatives displays a 14 °C thermal shift from native enzyme.