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Figure 7
Comparison of the allosteric binding sites in (a) PaFPPS (blue C atoms) and (b) HsFPPS (yellow C atoms). (a) The PaFPPS allosteric site with the two bound KM10833 molecules (NVU-1298 and NVU-1297). The location of the IPP binding site is illustrated by superimposition of the EcFPPS–IPP complex (PDB entry 1rqi ). (b) Three fragment ligands bound to FPPS are shown in ball-and-stick representation. One ligand (C atoms coloured yellow) is a representative example found to bind in the allosteric binding site of HsFPPS with an accompanying sulfate ion (PDB entry 3n5h ; Jahnke et al., 2010BB16). The other two (blue-coloured C atoms; NVU-1298/NVU-1297) are the superposed KM10833 from the PaFPPS complex shown in (a) (PDB entry 3zl6 ). Residues from each structure forming direct contacts are labelled.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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