1jsa: Difference between revisions
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|PDB= 1jsa |SIZE=350|CAPTION= <scene name='initialview01'>1jsa</scene> | |PDB= 1jsa |SIZE=350|CAPTION= <scene name='initialview01'>1jsa</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jsa OCA], [http://www.ebi.ac.uk/pdbsum/1jsa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jsa RCSB]</span> | |||
}} | }} | ||
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[[Category: Stryer, L.]] | [[Category: Stryer, L.]] | ||
[[Category: Tanaka, T.]] | [[Category: Tanaka, T.]] | ||
[[Category: calcium binding protein]] | [[Category: calcium binding protein]] | ||
[[Category: calcium-myristoyl switch]] | [[Category: calcium-myristoyl switch]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:16 2008'' | ||
Revision as of 18:38, 30 March 2008
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| 1jsa | |||||||||||||
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| Ligands: | CA, MYR | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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