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. 2014 Jul 22;2:50. doi: 10.3389/fchem.2014.00050

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Copyright © 2014 Park, Matralis, Berghuis and Tsantrizos.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Structure of geranylgeranyl pyrophosphate synthase. (A) The inter-dimer interface in hGGPPS (PDB ID: 2Q80). (B) Binding of a bisphosphonate with a long alkyl side chain to yeast GGPPS (PDB ID: 2Z4X); the trinuclear metal cluster is similar to that in Figure 4A. (C) The product chain elongation channel in hGGPPS. (D) Binding of the substrate FPP in yeast GGPPS (PDB ID: 2E90); conformational changes of the key residues (as compared to the same residues in C) are evident; also Ala59 in hGGPPS is replaced with a serine in yeast GGPPS. (E) Binding of GGPP at the product inhibitory site in hGGPPS.