Ternary complex structures of human farnesyl pyrophosphate synthase bound with a novel inhibitor and secondary ligands provide insights into the molecular details of the enzyme’s active site closure
1 Department of Biochemistry, McGill University, 3649 Promenade Sir William Osler, Montreal, QC, Canada
2 Department of Microbiology and Immunology, McGill University, 3649 Promenade Sir William Osler, Montreal, QC, Canada
3 Groupe de Recherche Axé sur la Structure des Protéines, McGill University, 3649 Promenade Sir William Osler, Montreal, QC, Canada
4 Department of Chemistry, McGill University, 801 Sherbrooke Street West, Montreal, QC, Canada
BMC Structural Biology 2012, 12:32 doi:10.1186/1472-6807-12-32Published: 12 December 2012
Additional file 1:
Table S1. Average B-factors for the overall structure and the four C-terminal residues of human FPPS complexes.
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Additional file 2:
Figure S1. Electron density maps and average B-factors for the residues involved in the human FPPS tail closure. The structure of the Pi-bound complex is represented in green, and that of the PPi-bound complex in cyan. The 2Fo-Fc maps for the residues of interest are contoured at 1.0 sigma level and shown in respective colors. The average B-factor for each residue was calculated only for the side chain. The overall B-factors of the two structures are very similar (Additional file 1: Table S1).
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