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Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state

Nature volume 376, pages 444–447 (1995)Cite this article

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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Author notes

  1. Timothy S. Harvey

    Present address: Molecular Structure Group, Amgen Inc., 1840 DeHavilland Drive, Thousand Oaks, California, 91320, USA

Authors and Affiliations

  1. Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 500 Sherbourne Street, Toronto, Ontario, M4X 1K9, Canada

    Toshiyuki Tanaka, Timothy S. Harvey & Mitsuhiko lkura

  2. Department of Neurobiology, Stanford University School of Medicine, Stanford, California, 94305, USA

    James B. Amest & Lubert Stryer

Authors
  1. Toshiyuki Tanaka
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  2. James B. Amest
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  3. Timothy S. Harvey
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  4. Lubert Stryer
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  5. Mitsuhiko lkura
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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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