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. Author manuscript; available in PMC: 2011 Mar 1.
Published in final edited form as: Proteins. 2010 Mar;78(4):888–899. doi: 10.1002/prot.22614

Figure 3. Alternative conformations of Tyr94 and Gln167 (Stereo view).

Figure 3

The conformations of Tyr94 and Gln167 are dependent on the size of the nitrogen-containing group in the bisphosphonate inhibitors. Tyr94, Gln167, and N-BPs are shown as sticks. The same color coding as in Figure 2C is used for different N-BPs. (A) In the structures of TcFPPS in complex with 91B, 261A, and 461A, where the nitrogen-containing groups are shorter, Tyr94 and Gln167 are closer to each other. (B) These two residues become more separated (by ~ 2.0 Å)accommodate the longer nitrogen-containing groups of 300B and 476A. (C) Superposition of the two conformational states of residues Tyr94 and Gln167, as well as the structure of human FPPS/zoledronate (PDB ID: 1ZW5, blue) 14.