1jsa
From Proteopedia
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MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES
Overview
Many eukaryotic cellular and viral proteins have a covalently attached, myristoyl group at the amino terminus. One such protein is recoverin, a, calcium sensor in retinal rod cells, which controls the lifetime of, photoexcited rhodopsin by inhibiting rhodopsin kinase. Recoverin has a, relative molecular mass of 23,000 (M[r] 23K), and contains an, amino-terminal myristoyl group (or related acyl group) and four EF hands., The binding of two Ca2+ ions to recoverin leads to its translocation from, the cytosol to the disc membrane. In the Ca2+-free state, the myristoyl, group is sequestered in a deep hydrophobic box, where it is clamped by, multiple residues contributed by three of the EF hands. We have used, nuclear magnetic resonance to show that Ca2+ induces the unclamping and, extrusion of the myristoyl group, enabling it to interact with a lipid, bilayer membrane. The transition is also accompanied by a 45-degree, rotation of the amino-terminal domain relative to the carboxy-terminal, domain, and many hydrophobic residues are exposed. The conservation of the, myristoyl binding site and two swivels in recoverin homologues from yeast, to humans indicates that calcium-myristoyl switches are ancient devices, for controlling calcium-sensitive processes.
About this Structure
1JSA is a Single protein structure of sequence from Bos taurus with CA and MYR as ligands. Full crystallographic information is available from OCA.
Reference
Molecular mechanics of calcium-myristoyl switches., Ames JB, Ishima R, Tanaka T, Gordon JI, Stryer L, Ikura M, Nature. 1997 Sep 11;389(6647):198-202. PMID:9296500
Page seeded by OCA on Tue Nov 20 18:32:29 2007
