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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

Jaeok Park1, Yih-Shyan Lin4, Joris W De Schutter4, Youla S Tsantrizos134 and Albert M Berghuis123*

Author Affiliations

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

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BMC Structural Biology 2012, 12:32  doi:10.1186/1472-6807-12-32

Published: 12 December 2012

Additional files

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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