1IKU
myristoylated recoverin in the calcium-free state, NMR, 22 structures
Summary for 1IKU
| Entry DOI | 10.2210/pdb1iku/pdb |
| Descriptor | RECOVERIN, MYRISTIC ACID (2 entities in total) |
| Functional Keywords | calcium-myristoyl switch, calcuim-binding protein, calcium-binding protein |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 23463.58 |
| Authors | Tanaka, T.,Ames, J.B.,Harvey, T.S.,Stryer, L.,Ikura, M. (deposition date: 1996-01-18, release date: 1996-07-11, Last modification date: 2024-11-13) |
| Primary citation | Tanaka, T.,Ames, J.B.,Harvey, T.S.,Stryer, L.,Ikura, M. Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature, 376:444-447, 1995 Cited by 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. PubMed: 7630423DOI: 10.1038/376444a0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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