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[[Image:2het.gif|left|200px]]


{{Structure
==Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to EF-hand 3==
|PDB= 2het |SIZE=350|CAPTION= <scene name='initialview01'>2het</scene>, resolution 3.0&Aring;
<StructureSection load='2het' size='340' side='right'caption='[[2het]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[2het]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HET FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
|GENE= RCV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2het FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2het OCA], [https://pdbe.org/2het PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2het RCSB], [https://www.ebi.ac.uk/pdbsum/2het PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2het ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/he/2het_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2het ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.


'''Non-myristoylated bovine recoverin (truncated at C-terminus) with calcium bound to EF-hand 3'''
Tuning of a neuronal calcium sensor.,Weiergraber OH, Senin II, Zernii EY, Churumova VA, Kovaleva NA, Nazipova AA, Permyakov SE, Permyakov EA, Philippov PP, Granzin J, Koch KW J Biol Chem. 2006 Dec 8;281(49):37594-602. Epub 2006 Oct 2. PMID:17015448<ref>PMID:17015448</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2het" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Recoverin is a Ca(2+)-regulated signal transduction modulator expressed in the vertebrate retina that has been implicated in visual adaptation. An intriguing feature of recoverin is a cluster of charged residues at its C terminus, the functional significance of which is largely unclear. To elucidate the impact of this segment on recoverin structure and function, we have investigated a mutant lacking the C-terminal 12 amino acids. Whereas in myristoylated recoverin the truncation causes an overall decrease in Ca(2+) sensitivity, results for the non-myristoylated mutant indicate that the truncation primarily affects the high affinity EF-hand 3. The three-dimensional structure of the mutant has been determined by x-ray crystallography. In addition to significant changes in average coordinates compared with wild-type recoverin, the structure provides strong indication of increased conformational flexibility, particularly in the C-terminal domain. Based on these observations, we propose a novel role of the C-terminal segment of recoverin as an internal modulator of Ca(2+) sensitivity.
*[[Recoverin%2C a calcium-activated myristoyl switch|Recoverin%2C a calcium-activated myristoyl switch]]
 
== References ==
==About this Structure==
<references/>
2HET is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HET OCA].
__TOC__
 
</StructureSection>
==Reference==
Tuning of a neuronal calcium sensor., Weiergraber OH, Senin II, Zernii EY, Churumova VA, Kovaleva NA, Nazipova AA, Permyakov SE, Permyakov EA, Philippov PP, Granzin J, Koch KW, J Biol Chem. 2006 Dec 8;281(49):37594-602. Epub 2006 Oct 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17015448 17015448]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Granzin, J.]]
[[Category: Granzin J]]
[[Category: Weiergraber, O H.]]
[[Category: Weiergraber OH]]
[[Category: CA]]
[[Category: calcium binding]]
[[Category: ef-hand]]
[[Category: helix-loop-helix]]
[[Category: recoverin]]
 
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