Farnesyl diphosphate synthase: Difference between revisions
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== Structure == | == Structure == | ||
FPPS exists as a homodimer, with each monomer having an active site. The monomers have the characteristic FPPS fold of a ten-helix bundle and four other helices that run perpendicular to the bundle. There are two substrate sites, one is allylic and the other is homoallylic. GPP and DMAPP bind to the allylic site, while IPP binds to the homoallylic site. These two sites are connected to the top of the bundle and exist as part of a cavity<ref>PMID:24598749</ref>. | FPPS exists as a homodimer, with each monomer having an active site. The monomers have the characteristic FPPS fold of a ten-helix bundle and four other helices that run perpendicular to the bundle. There are two substrate sites, one is allylic and the other is homoallylic. GPP and DMAPP bind to the allylic site, while IPP binds to the homoallylic site. These two sites are connected to the top of the bundle and exist as part of a cavity<ref>PMID:24598749</ref>. Another characteristic feature of all FPPS enzymes are two highly conserved aspartate rich motifs. These motifs are called <scene name='48/485622/Lmfpps_rbs/5'>First Aspartate Rich Motif (FARM) and Second Aspartate Rich Motif (SARM)</scene>, and have sequences of DDXX(XX)D and DDXXD respectively. FARM and SARM are found on opposite sides on the active site cavity facing one another<ref>DOI: 10.1021/acs.biochem.0c00432</ref>. | ||
When FPPS interacts with bisphosphonates, the bisphosphonates bind in the homoallylic binding sites and are coordinated by three divalent cations (Ca 2+ or Mg 2+). | When FPPS interacts with bisphosphonates, the bisphosphonates bind in the homoallylic binding sites and are coordinated by three divalent cations (Ca 2+ or Mg 2+). | ||
