Sandbox Reserved 1066: Difference between revisions
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== ''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase == | == ''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase == | ||
''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase, also known as FadD13, is unique within its class in regards to its ability to house lipid substrates longer than itself. Most FadD class proteins exist as integral membrane proteins involved in lipid transport into the cell. FadD13 is unique structurally in that it exists as a peripheral protein on the inside of the cell membrane. This feature is key in the mechanistic basis for FadD13's transport of fatty acids of length C24-C26. | ''Mycobacterium tuberculosis'' very-long-chain fatty acyl-CoA synthetase, also known as FadD13, is unique within its class in regards to its ability to house lipid substrates longer than itself. Most FadD class proteins exist as integral membrane proteins involved in lipid transport into the cell. FadD13 is unique structurally in that it exists as a peripheral protein on the inside of the cell membrane. This feature is key in the mechanistic basis for FadD13's transport of fatty acids of length C24-C26.<ref name="Our Paper">PMID: 22560731</ref> | ||
FadD13 may be important in the virulence of [https://en.wikipedia.org/wiki/Tuberculosis tuberculosis] and has emerged as possible target for therapeutic agents. | FadD13 may be important in the virulence of [https://en.wikipedia.org/wiki/Tuberculosis tuberculosis] and has emerged as possible target for therapeutic agents. | ||
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This is the <scene name='69/698726/Overall_structure_cartoon/1'>overall structure of FadD13</scene> | This is the <scene name='69/698726/Overall_structure_cartoon/1'>overall structure of FadD13</scene> | ||
FadD13 is composed of 503 amino acid residues divided into three main regions: The <scene name='69/694233/Domains/1'>N-terminal domain</scene> (residues 1-395) and <scene name='69/694233/C-terminal_domain/1'>C-terminal domain</scene> (residues 402-503) which are connected via a flexible linker (residues 396-401). | FadD13 is composed of 503 amino acid residues divided into three main regions: The <scene name='69/694233/Domains/1'>N-terminal domain</scene> (residues 1-395) and <scene name='69/694233/C-terminal_domain/1'>C-terminal domain</scene> (residues 402-503) which are connected via a flexible linker (residues 396-401).<ref name="OUR PAPER"/> | ||
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== Hydrophobic Tunnel == | == Hydrophobic Tunnel == | ||
The hydrophobic tunnel of FadD13 is essential to the transport and accommodation of very long fatty acids from the membrane into the cell. This | The hydrophobic tunnel 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.<ref name="OUR PAPER"/> | ||
== Active Site == | == Active Site == | ||
