1jsa

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(New page: 200px<br /><applet load="1jsa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jsa" /> '''MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BO...)
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[[Image:1jsa.gif|left|200px]]<br /><applet load="1jsa" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jsa" />
 
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'''MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES'''<br />
 
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==Overview==
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==MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES==
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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.
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<StructureSection load='1jsa' size='340' side='right'caption='[[1jsa]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jsa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JSA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 24 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jsa OCA], [https://pdbe.org/1jsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jsa RCSB], [https://www.ebi.ac.uk/pdbsum/1jsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jsa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RECO_BOVIN RECO_BOVIN] Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.<ref>PMID:8097896</ref> <ref>PMID:8392055</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/js/1jsa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jsa ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:9296500</ref>
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1JSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JSA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9296500 9296500]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1jsa" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Ames, J.B.]]
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[[Category: Gordon, J.I.]]
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[[Category: Ikura, M.]]
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[[Category: Ishima, R.]]
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[[Category: Stryer, L.]]
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[[Category: Tanaka, T.]]
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[[Category: CA]]
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[[Category: MYR]]
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[[Category: calcium binding protein]]
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[[Category: calcium-myristoyl switch]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:32:29 2007''
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==See Also==
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*[[Recoverin%2C a calcium-activated myristoyl switch|Recoverin%2C a calcium-activated myristoyl switch]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Ames JB]]
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[[Category: Gordon JI]]
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[[Category: Ikura M]]
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[[Category: Ishima R]]
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[[Category: Stryer L]]
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[[Category: Tanaka T]]

Current revision

MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES

PDB ID 1jsa

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