Sandbox Reserved 1132: Difference between revisions
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== Structure == | == Structure == | ||
FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of <scene name='71/719873/Phe_113/1'>Phe-113</scene> limits the cavity on one site. The helices α4 and α8 contain highly conserved and <scene name='71/719873/Aspartate-rich_motives/1'>aspartate-rich motives</scene> (<sup>103</sup>DDIUD<sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of Lys-200 in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref> | FPPS is a dimer made of two identical subunits, which each contain 13 α-helices and connecting loops. The regions which connect the helices α4-α5 and α8-α9 are extended. Within the handle of helices FPPS has a large central cavity, which acts as a hydrophobic ligand-binding site. The site-chain of <scene name='71/719873/Phe_113/1'>Phe-113</scene> limits the cavity on one site. The helices α4 and α8 contain highly conserved and <scene name='71/719873/Aspartate-rich_motives/1'>aspartate-rich motives</scene> (<sup>103</sup>DDIUD<sup>107</sup> and <sup>243</sup>DDYLD<sup>247</sup>). A distinctive kink in helix α7 turns carbonyl of <scene name='71/719873/Lys-200/1'>Lys-200</scene> in the direction of the cavity.<ref name = "paper1"> PMID: 16684881 </ref> | ||