1JSA

MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES

Summary for 1JSA

• Entry DOI: 10.2210/pdb1jsa/pdb
• NMR Information: BMRB: 5332
• Descriptor: RECOVERIN, CALCIUM ION, MYRISTIC ACID (3 entities in total)
• Functional Keywords: calcium binding protein, calcium-myristoyl switch, calcium binding
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 1
• Total formula weight: 23543.74

Authors

Ames, J.B.,Ishima, R.,Tanaka, T.,Gordon, J.I.,Stryer, L.,Ikura, M. (deposition date: 1997-06-04, release date: 1997-10-15, Last modification date: 2024-10-16)

Primary citation

Ames, J.B.,Ishima, R.,Tanaka, T.,Gordon, J.I.,Stryer, L.,Ikura, M.
Molecular mechanics of calcium-myristoyl switches.
Nature, 389:198-202, 1997

PubMed Abstract: 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.

PubMed: 9296500
DOI: 10.1038/38310

Experimental method

SOLUTION NMR