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

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Eric Martz, Eran Hodis, Michal Harel, Alexander Berchansky, Joel L. Sussman, Karsten Theis

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 <applet load='Recoverin_linear_morph14.pdb' scene='Recoverin,_a_calcium-activated_myristoyl_switch/Recoverin_no_calcium/2' size='400' frame='true' align='right' caption='Recoverin: 1iku model 7 morphed to 1jsa model 9.' />
-Recoverin 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.
+Recoverin (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.
 The two calcium ions each bind to an EF hand motif, one in the C-terminal domain, and one in the N-terminal domain. Recoverin actually contains four EF hand motifs, but two of them are unable to bind calcium due to variations in sequence.