Sandbox Reserved 1066: Difference between revisions

The ability for FadD13 to transport and activate fatty acids of the maximum tested length C26, lies in it being a peripheral membrane protein. FadD13's attachment to the membrane via electrostatic interactions in the N-terminal domain is coupled with the presence of a hydrophobic tunnel located centrally in this same domain. This method of attachment, with the alignment of the hydrophobic tunnel to the membrane, allows the extension of these very-long-chain fatty acids to enter FadD13 from the membrane (Figure 1).  Of importance to the passage of these fatty acid substrates into FadD13 resides in the presence of an arginine rich lid-loop, located at the top of the hydrophobic tunnel and embedded in the membrane, which serves to block the transport of fatty acids into the enzyme. Once the lid-loop is opened, fatty acids may be pulled from the membrane into a hydrophobic tunnel, which is the main structural component by which fatty acids are transported from the membrane into the cel (Figure 1).