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Figure 2
Residues of the FPPS tail closure. (a) Tail closure induced by IPP binding. The hFPPS–YS0470–2Pi complex (cyan) and the hFPPS–YS0470–IPP complex (magenta) are superposed, with the bound ligands omitted for clarity. Note that the hFPPS–YS0470–2Pi complex is missing the C-terminal tail, which in the hFPPS–YS0470–IPP complex (highlighted in black) closes over the active-site entrance. The structures are shown in approximately the same orientation as in Fig. 1[link](e) (compare residues Lys57, Asn59 and Arg60). (b) The conformational change cascade required for the tail closure. In the absence of bound IPP/PPi, Tyr349 is trapped in the `off' conformation by π-stacking and hydrogen-bond interactions. The `off' conformations of Tyr349, Phe238 and Gln242 (cyan) prohibit the `on' conformations of Phe238, Gln242 and Arg351 (magenta), respectively, by steric hindrance. (c) A second ligand-free T. brucei FPPS complex (PDB entry 3dyh , white) with its ordered C-terminal tail. (d) Conserved residues of the FPPS tail closure. Sequence alignment was carried out with ClustalX (Larkin et al., 2007BB14).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 70| Part 3| February 2014| Pages 299-304
doi:10.1107/S2053230X14002106
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