Recoverin, a calcium-activated myristoyl switch: Difference between revisions

<scene name='Recoverin,_a_calcium-activated_myristoyl_switch/Recoverin_no_calcium/2'>Recoverin</scene> (Initial colors: '''<font color="#808080">Hydrophobic</font>, <font color="#e000e0">Polar</font>''') has a <scene name='Recoverin,_a_calcium-activated_myristoyl_switch/Recoverin_morph/5'>myristic acid</scene> (14-carbon saturated fatty acid, or a similar acyl moiety) covalently linked via an amide bond to its N-terminal glycine. In the absence of calcium, the <scene name='Recoverin,_a_calcium-activated_myristoyl_switch/Recoverin_no_calcium/1'>myristoyl group is buried</scene> in the N-terminal protein domain, surrounded on all sides by alpha helices that form a hydrophobic pocket. The binding of <scene name='Recoverin,_a_calcium-activated_myristoyl_switch/Recoverin_morph/6'>two calcium ions</scene> to each recoverin molecule induces a <scene name='Recoverin,_a_calcium-activated_myristoyl_switch/Recoverin_morph/1'>conformational change </scene> that extrudes the myristoyl and exposes some hydrophobic amino acids on the surface. This enables the molecule to bind to the lipid bilayers of the disc membranes.

Both 1iku and 1jsa are ensembles of NMR models. The morph is a [[Morphs |linear interpolation morph]] between model 7 and model 9, respectively. Only the alpha carbon atoms of the protein are present in the morph PDB file. For the space-filled model 7 of 1iku, hydrogen atoms were deleted except for those in the myristoyl adduct.