1IKU | pdb_00001iku

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

(1995) Nature 376: 444-447

• PubMed: 7630423 Search on PubMed
• DOI: https://doi.org/10.1038/376444a0
• Primary Citation of Related Structures:  
  1IKU


• PubMed Abstract: 
  

  Recoverin, a retinal calcium-binding protein of relative molecular mass (M(r)) 23K, participates in the recovery phase of visual excitation and in adaptation to background light. The Ca(2+)-bound form of recoverin prolongs the photoresponse, probably by blocking phosphorylation of photoexcited rhodopsin. Retinal recoverin contains a covalently attached myristoyl group or related acyl group at its amino terminus and two Ca(2+)-binding sites. 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). Here we present the solution structure of Ca(2+)-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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Organizational Affiliation: 

Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.