Farnesyl diphosphate synthase

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Revision as of 23:03, 20 January 2016

Human farnesyl diphosphate synthase tetramer complex with lipophylic bisphosphonate inhibitor and Mg+2 ions (green) (PDB code 2opm)

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Updated on 20-January-2016

↑ Schulbach MC, Mahapatra S, Macchia M, Barontini S, Papi C, Minutolo F, Bertini S, Brennan PJ, Crick DC. Purification, enzymatic characterization, and inhibition of the Z-farnesyl diphosphate synthase from Mycobacterium tuberculosis. J Biol Chem. 2001 Apr 13;276(15):11624-30. Epub 2001 Jan 4. PMID:11152452 doi:http://dx.doi.org/10.1074/jbc.M007168200

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-<StructureSection load='2opm' size='350' side='right' scene='' caption='Human farnesyl diphosphate synthase tetramer complex with  lipophylic bisphosphonate inhibitor (PDB code [[2opm]]) '>
+<StructureSection load='2opm' size='350' side='right' scene='' caption='Human farnesyl diphosphate synthase tetramer complex with  lipophylic bisphosphonate inhibitor and Mg+2 ions (green) (PDB code [[2opm]]) '>
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+== Function ==
 '''Farnesyl diphosphate synthase''' (FPS) also named farnesyl pyrophosphate synthase catalyzes the conversion of geranyl diphosphate (GDP) and isopentenyl diphosphate (IPP) to farnesyl diphosphate and diphosphate<ref>PMID:11152452</ref>.
+== Structural insights ==
+FPS active site contains Mg<sup>+2</sup> ions and binds bisphosphonate inhibitors.
 </StructureSection>
 ==3D structures of farnesyl diphosphate synthase==