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1jsa
From Proteopedia
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[[Image:1jsa.gif|left|200px]] | [[Image:1jsa.gif|left|200px]] | ||
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'''MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES''' | '''MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES''' | ||
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[[Category: Stryer, L.]] | [[Category: Stryer, L.]] | ||
[[Category: Tanaka, T.]] | [[Category: Tanaka, T.]] | ||
| - | [[Category: | + | [[Category: Calcium binding protein]] |
| - | [[Category: | + | [[Category: Calcium-myristoyl switch]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:49:53 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:49, 2 May 2008
MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES
Overview
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.
About this Structure
1JSA is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Molecular mechanics of calcium-myristoyl switches., Ames JB, Ishima R, Tanaka T, Gordon JI, Stryer L, Ikura M, Nature. 1997 Sep 11;389(6647):198-202. PMID:9296500 Page seeded by OCA on Fri May 2 21:49:53 2008
