Abstract
RECOVERIN, a retinal calcium-binding protein of relative molecular mass (Mr) 23K, participates in the recovery phase of visual excitation and in adaptation to background light1–3. The C a2 +-bound form of recoverin prolongs the photoresponse4, probably by blocking phosphorylation of photoexcited rhodopsin5. Retinal recoverin contains a covalently attached myristoyl group or related acyl group at its amino terminus6 and two Ca2+ -binding sites7. Ca2+ binding to myristoylated, but not unmyristoylated, recoverin induces its translocation to bilayer membranes, indicating that the myristoyl group is essential to the read-out of calcium signals (calcium-myristoyl switch)8,9. Here we present the solution structure of Ca2+-free, myristoylated recombinant recoverin obtained by heteronuclear multidimensional NMR spectroscopy. The myristoyl group is sequestered in a deep hydrophobic pocket formed by many aromatic and other hydrophobic residues from five flanking helices.
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Tanaka, T., Amest, J., Harvey, T. et al. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376, 444–447 (1995). https://doi.org/10.1038/376444a0
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DOI: https://doi.org/10.1038/376444a0
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