1jsa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1jsa.gif|left|200px]]
[[Image:1jsa.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1jsa |SIZE=350|CAPTION= <scene name='initialview01'>1jsa</scene>
+
The line below this paragraph, containing "STRUCTURE_1jsa", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1jsa| PDB=1jsa | SCENE= }}
-
|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>
+
-
}}
+
'''MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES'''
'''MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES'''
Line 31: Line 28:
[[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 Fri May 2 21:49:53 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:16 2008''
+

Revision as of 18:49, 2 May 2008

Template:STRUCTURE 1jsa

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools