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. <scene name='24/241531/Recoverin_storymorph/1'>An alternate morph</scene> <ref>The [[Jmol/Storymorph|Storymorph Jmol scripts]] were used to create the interpolation shown in the morph. [https://proteopedia.org/wiki/index.php/Image:Morph_recoverin.pdb Coordinates] available on Proteopedia</ref> emphasizes that two parts of the molecule rotate relative to each other while retaining their local fold.