Sandbox Reserved 1066: Difference between revisions
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=Structure = | =Structure = | ||
FadD13 is composed of 503 amino acid residues divided into three main regions: The <scene name='69/694233/N_terminal_domain/1'>N-terminal domain</scene> (residues 1-395) and <scene name='69/694233/C-terminal_domain/2'>C-terminal domain</scene> (residues 402-503) which are connected via a flexible <scene name='69/694233/Linker_section/2'>linker</scene> represented in dark blue (residues 396-401).<ref name="Our Paper"/> Each region plays an important role in the activation of fatty acids. The large N-terminal domain houses many key structural features involved in fatty acid activation, but ultimately it is the flexible linker that allows movement of the C-terminal domain to from the fully functioning active site of FadD13 (Figure 1). | FadD13 is composed of 503 amino acid residues divided into three main regions: The <scene name='69/694233/N_terminal_domain/1'>N-terminal domain</scene> (residues 1-395) and <scene name='69/694233/C-terminal_domain/2'>C-terminal domain</scene> (residues 402-503) which are connected via a flexible <scene name='69/694233/Linker_section/2'>linker</scene> represented in dark blue (residues 396-401).<ref name="Our Paper"/> Each region plays an important role in the activation of fatty acids. The large N-terminal domain houses many key structural features involved in fatty acid activation, but ultimately it is the flexible linker that allows movement of the C-terminal domain to from the fully functioning active site of FadD13 (Figure 1). | ||
== Electrostatics == | == Electrostatics == | ||
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== Hydrophobic Tunnel == | == Hydrophobic Tunnel == | ||
The <scene name='69/694233/Hydrophobic_tunnel/ | The <scene name='69/694233/Hydrophobic_tunnel/2'>hydrophobic tunnel</scene> of FadD13 is essential to the transport and accommodation of very long fatty acids from the membrane into the cell. This tunnel runs through the middle of FadD13 from the arginine rich lid loop to the ATP binding site and is situated between the and alpha helices α8-α9 and parallel beta sheet β9- β14 (Figure 4).<ref name="Our Paper"/> Negatively charged residues at the active site of FadD13 are the driving factor in the attraction of the fatty acid from the membrane through the hydrophobic tunnel of the enzyme. | ||
[[Image:Hydrophobic tunnel 2.jpg|300 px|left|thumb|Figure 4: Pmyol depiction of hydrophobic tunnel.]] | [[Image:Hydrophobic tunnel 2.jpg|300 px|left|thumb|Figure 4: Pmyol depiction of hydrophobic tunnel.]] | ||
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==References== | ==References== | ||
<references/> | <references/> | ||
